Tlr3 binding bicyclic peptide ligands

Abstract

The present invention relates to peptide ligands which are capable of binding to TLR3. In particular, the invention describes bicyclic peptide ligands which comprise a peptide ligand as described herein, and a molecular scaffold, wherein the three cysteine residues of said peptide ligand form covalent bonds with the molecular scaffold to form two loop sequences. The invention also includes pharmaceutical compositions, multimeric binding complexes and drug conjugates comprising said peptide ligands and the use of said peptide ligands in preventing, suppressing or treating diseases or disorders mediated by TLR3, such as autoimmune diseases, inflammatory conditions and cancer.

Description

[0001] TLR3 BINDING BICYCLIC PEPTIDE LIGANDS FIELD OF THE INVENTION The present invention relates to peptide ligands which are capable of binding to TLR3. In particular, the invention describes bicyclic peptide ligands which comprise a peptide ligand as described herein, and a molecular scaffold, wherein the three reactive groups (for example cysteine residues) of said peptide ligand form covalent bonds with the molecular scaffold to form two loop sequences. The invention also includes pharmaceutical compositions, multimeric binding complexes and drug conjugates comprising said peptide ligands and the use of said peptide ligands in preventing, suppressing or treating diseases or disorders mediated by TLR3, such as autoimmune diseases, inflammatory conditions and cancer. BACKGROUND OF THE INVENTION Cyclic peptides are able to bind with high affinity and target specificity to protein targets and hence are an attractive molecule class for the development of therapeutics. In fact, several cyclic peptides are already successfully used in the clinic, as for example the antibacterial peptide vancomycin, the immunosuppressant drug cyclosporine or the anti-cancer drug octreotide (Driggers et al. (2008), Nat Rev Drug Discov 7 (7), 608-24). Good binding properties result from a relatively large interaction surface formed between the peptide and the target as well as the reduced conformational flexibility of the cyclic structures. Typically, macrocycles bind to surfaces of several hundred square angstrom, as for example the cyclic peptide CXCR4 antagonist CVX15 (400 Å2; Wu et al. (2007), Science 330, 1066-71), a cyclic peptide with the Arg-Gly-AsS^PRWLI^ELQGLQJ^WR^LQWHJULQ^Į9E^^^^^^^c2) (Xiong et al. (2002), Science 296 (5565), 151-5) or the cyclic peptide inhibitor upain-1 binding to urokinase-type plasminogen activator (603 Å2; Zhao et al. (2007), J Struct Biol 160 (1), 1-10). Due to their cyclic configuration, peptide macrocycles are less flexible than linear peptides, leading to a smaller loss of entropy upon binding to targets and resulting in a higher binding affinity. The reduced flexibility also leads to locking target-specific conformations, increasing binding specificity compared to linear peptides. This effect has been exemplified by a potent and selective inhibitor of matrix metalloproteinase 8 (MMP-8) which lost its selectivity over other MMPs when its ring was opened (Cherney et al. (1998), J Med Chem 41 (11), 1749-51). The favorable binding properties achieved through macrocyclization are even more pronounced in multicyclic peptides having more than one peptide ring as for example in vancomycin, nisin and actinomycin. Different research teams have previously tethered polypeptides with cysteine residues to a synthetic molecular structure (Kemp and McNamara (1985), J. Org. Chem; Timmerman et al. (2005), ChemBioChem). Meloen and co-workers had used tris(bromomethyl)benzene and related molecules for rapid and quantitative cyclisation of multiple peptide loops onto synthetic scaffolds for structural mimicry of protein surfaces (Timmerman et al. (2005), ChemBioChem). Methods for the generation of candidate drug compounds wherein said compounds are generated by linking cysteine containing polypeptides to a molecular scaffold as for example tris(bromomethyl)benzene are disclosed in WO 2004 / 077062 and WO 2006 / 078161. Phage display-based combinatorial approaches have been developed to generate and screen large libraries of bicyclic peptides to targets of interest (Heinis et al. (2009), Nat Chem Biol 5 (7), 502-7 and WO 2009 / 098450). Briefly, combinatorial libraries of linear peptides containing three cysteine residues and two regions of six random amino acids (Cys-(Xaa)6-Cys-(Xaa)6- Cys) were displayed on phage and cyclised by covalently linking the cysteine side chains to a small molecule scaffold. SUMMARY OF THE INVENTION According to a first aspect of the invention, there is provided a peptide ligand comprising a polypeptide having an amino acid sequence selected from: C-X1-X2-X3-C-X4-X5-X6-X7-X8-X9-C (SEQ ID NO: 1); C-X10-X11-Y-Y-C-X12-Q-T-X13-X14-F-C (SEQ ID NO: 2); X15-X16-X17-X18-X19-X20-X21-X22-X23-X24-X25-X26-X27-X28-X29(SEQ ID NO: 3); C-Q-P-T-X30-X31-C-X32-X33-X34-X35-X36-X37-C (SEQ ID NO: 4); C-Y-Y-X38-X39-X40-Y-A-C-L-D-C (SEQ ID NO: 5); and X41-X42-X43-X44-X45-X46-X47-X48-X49-C-X50-X51-X52-X53-X54(SEQ ID NO: 6); wherein: X1represents D, N, P, Y, 26DiMeTyr, 2FTyr, 3FTyr, or 4FPhe; X2represents A, I, N, P, S, T, Aze, Cba, Cis-HyP, tBuAla, or tBuGly; X3represents A, G, N, P, Q, R, Aib, Aze, Cis-HyP, dA, HyP, or Pip; X4represents L, S, or Cba; X5represents K, P, R, W, 5FTrp, 5MeOTrp, 6ClTrp, 6FTrp, 6MeTrp, Agb, HArg, Trp(Me), or Trp(S); X6represents M, R, or HArg; X7represents A, F, Q, Y, 2FTyr, 3FTyr, 3tBuTyr, or 4FPhe; X8represents H, I, N, V, Cbg, His1Me, His3Me, or tBuGly; X9 represents D, F, L, 1Nal, 2Nal, 4tBuPhe, Cba, or tBuAla; X10represents S or T; X11represents K or S; X12represents E or Q; X13represents R or V; X14represents H or R; X15represents C or dC; X16represents A, D, H, I, L, M, N, P, S, T, W, CF3Nva, dP, HyP, Nle, Nva, or TfNle; X17represents E, L, N, P, Q, S, T, Y, 26DiMeTyr, Cba, dL, or tBuAla; X18represents D, E, L, P, R, T, Agb, Cba, Cit, dD, HArg, or tBuAla; X19represents A, E, I, L, M, Q, V, AlloIle, Cba, CF3Ala, dL, HLeu, Nle, or tBuAla; X20represents C or dC; X21represents A, E, F, L, Q, R, T, W, Y, 1Nal, 2FPhe, 2MePhe, 2Nal, 3FPhe, 3MePhe, 4FPhe, 4MePhe, or dE; X22represents A, R, V, Y, 26DiMeTyr, 2FTyr, 3FTyr, 3tBuTyr, 4FPhe, DOPA, or dY; X23represents A, D, W, 1Nal, 2Nal, 4MeoTrp, 5FTrp, dW, Gla, or Trp(S); X24represents A, D, E, H, M, Q, S, Y, dS, K(PYA), or Nle; X25represents E, F, L, N, S, T, V, Cba, or dS; X26represents R, W, Y, 1Nal, 2FTyr, 2MeTrp, 2Nal, 3FTyr, 4FTrp, 5FTrp, 5MeTrp, 6FTrp, 6MeTrp, 7FTrp, 7MeTrp, Cit, dR, HArg, or Trp(Me); X27represents G, R, S, Agb, Cit, dA, dE, or HArg; X28represents L, P, 44DFP, 4FlPro, Aze, Cba, dL, HyP, Pip, tBuAla, or trans-4FlPro; X29represents C, dC, or Cysam; X30represents P, Cis-HyP, HyP, or Pip; X31represents E, Q, or R; X32represents P, Aze, Cis-HyP, or HyP; X33represents F, Y, 2FTyr, 2Nal, 3FTyr, 4FPhe, or 4tBuPhe; X34represents N, S, or Dap; X35represents T or Dap; X36represents W, 1Nal, 2Nal, 4MeoTrp, 5FTrp, 5MeoTrp, 6ClTrp, 6FTrp, AzaTrp, or Trp(S); X37represents P, Aze, Cis-HyP, HyP, or Pip; X38represents E or P; X39represents D or N; X40represents W or Y; X41represents C or dC; X42represents A, D, E, G, K, N, P, S, T, V, Y, 3HyV, Aib, CF3Ala, dA, Dap, dK(PYA), dS, HSer, or K(PYA); X43represents N, T, or 3HyV; X44represents D, E, P, 4FlPro, Cis-Hyp, HyP, or trans-4FlPro; X45represents A, H, M, Q, S, V, Y, 1Nal, 26DiMeTyr, 2FTyr, 2Nal, 3FTyr, 4FPhe, DOPA, or HSer; X46represents A, E, F, I, M, V, 2FPhe, 4CF3Phe, Cba, CF3Nva, Nle, Nva, tBuAla, or TfNle; X47represents A, E, S, T, W, 1Nal, 2MeTrp, 4FTrp, 4MeTrp, 5FTrp, 5MeTrp, 6FTrp, 6MeTrp, 7FTrp, 7MeTrp, AzaTrp, CF3Ala, or Dap; X48represents K, R, Y, 2FTyr, 3FTyr, Agb, DOPA, HArg, or Orn; X49represents A, D, L, V, W, 1Nal, 2Nal, 3HyV, 4FTrp, 5FTrp, 5MeoTrp, 6FTrp, AzaTrp, C5g, Cbg, tBuGly, or Trp(S); X50represents E, M, Q, R, S, T, Arg(Me), Dap, HArg, or PG; X51represents A, E, K, M, R, S, T, 3HyV, Cit, HArg, or Orn; X52represents A, G, L, M, N, P, Q, Cba, dA, dK(PYA), K(PYA), Nle, Nva, R- aMeLys(PYA), S-aMeLys(PYA), or tBuAla; X53represents D, I, L, M, V, EPA, Nle, Nva, or tBuGly; and X54represents C, dC, or Cysam; or a modified derivative and / or pharmaceutically acceptable salt thereof. According to a further aspect of the invention, there is provided a bicyclic peptide ligand capable of binding TLR3, or a pharmaceutically acceptable salt thereof, which comprises a peptide ligand comprising a polypeptide comprising three reactive groups, (for example a peptide ligand as described herein), wherein the polypeptide is attached to a molecular scaffold According to a further aspect of the invention, there is provided a pharmaceutical composition which comprises the peptide ligand or bicyclic peptide ligand as described herein, in combination with one or more pharmaceutically acceptable excipients. According to a further aspect of the invention, there is provided a multimeric binding complex which comprises at least two bicyclic peptide ligands as defined herein, wherein said peptide ligands may be the same or different. According to a further aspect of the invention, there is provided a drug conjugate comprising a peptide ligand, bicyclic peptide ligand or multimeric binding complex as described herein, conjugated to one or more effector and / or functional groups. According to a further aspect of the invention, there is provided the peptide ligand, bicyclic peptide ligand, pharmaceutical composition, multimeric binding complex, or drug conjugate as described herein, for use in for use in preventing, suppressing or treating a disease or disorder mediated by TLR3. BRIEF DESCRIPTION OF THE FIGURES Figure 1: Images of monocyte-derived macrophages following incubation with selected bicyclic peptides of the invention. DETAILED DESCRIPTION OF THE INVENTION Definitions Unless specifically defined herein, all terms used herein have the same meaning as they would to one skilled in the art of the present invention. Practitioners are particularly directed to Sambrook et al., Molecular Cloning: A Laboratory Manual, 4th ed., Cold Spring Harbor Press, Plainsview, New York (2012); and Ausubel et al., Current Protocols in Molecular Biology (Supplement 114), John Wiley & Sons, New York (2016), for definitions and terms of the art. 7KH^WHUP^³DPLQR^DFLG´^LQ^WKH^FRQWH[W^RI^WKH^SUHVHQW^GLVFORVXUH^LV^XVHG^LQ^LWV^EURDGHVW^VHQse and is meant to include organic compounds containing amine (NH2) and carboxyl (COOH) functional groups, along with a side chain (e.g., a R group) specific to each amino acid. In VRPH^HPERGLPHQWV^^WKH^DPLQR^DFLGV^UHIHU^WR^QDWXUDOO\^RFFXUULQJ^ / ^Į-amino acids or residues. The commonly used one and three letter abbreviations for naturally occurring amino acids are used herein: A=Ala; C=Cys; D=Asp; E=Glu; F=Phe; G=Gly; H=His; I=Ile; K=Lys; L=Leu; M=Met; N=Asn; P=Pro; Q=Gln; R=Arg; S=Ser; T=Thr; V=Val; W=Trp; and Y=Tyr (Lehninger, A. L., (1975) Biochemistry, 2d ed., pp.71-92, Worth Publishers, New York). The general term ³DPLQR^DFLG´^IXUWKHU^LQFOXGHV^'-amino acids, retro-inverso amino acids as well as chemically modified amino acids such as amino acid analogues, naturally occurring amino acids that are not usually incorporated into proteins such as norleucine, and chemically synthesised compounds having properties known in the art to be characteristic of an amino acid, such as ȕ-amino acids. For example, analogues or mimetics of phenylalanine or proline, which allow the same conformational restriction of the peptide compounds as do natural Phe or Pro, are included within the definition of amino acid. Such analogues and mimetics are referred to herein as "functional equivalents" of the respective amino acid. Other examples of amino acids are listed by Roberts and Vellaccio, The Peptides: Analysis, Synthesis, Biology, Gross and Meiehofer, eds., Vol.5 p.341, Academic Press, Inc., N.Y.1983, which is incorporated herein by reference. The chemical properties of the 20 main amino acids are provided in Table A below. Table A - Chemical properties of amino acids Ala aliphatic, hydrophobic, neutral Met hydrophobic, neutral Cys polar, hydrophobic, neutral Asn polar, hydrophilic, neutral Asp polar, hydrophilic, charged (-) Pro hydrophobic, neutral Glu polar, hydrophilic, charged (-) Gln polar, hydrophilic, neutral Phe aromatic, hydrophobic, neutral Arg polar, hydrophilic, charged (+) Gly aliphatic, neutral Ser polar, hydrophilic, neutral His aromatic, polar, hydrophilic, Thr polar, hydrophilic, neutral charged (+) Ile aliphatic, hydrophobic, neutral Val aliphatic, hydrophobic, neutral Lys polar, hydrophilic, charged(+) Trp aromatic, hydrophobic, neutral Leu aliphatic, hydrophobic, neutral Tyr aromatic, polar, hydrophobic 7KH^ WHUPV^³SRO\SHSWLGH´^^DQG^ ³SHSWLGH´^´SHSWLGH^ OLJDQG´ are interchangeably used herein to refer to a polymer of amino acid residues and to variants and synthetic analogues of the same. Thus, these terms apply to amino acid polymers in which one or more amino acid residues is a synthetic non-naturally occurring amino acid, such as a chemical analogue of a corresponding naturally occurring amino acid, as well as to naturally-occurring amino acid polymers. Polypeptides can also undergo maturation or post-translational modification processes that may include, but are not limited to: glycosylation, proteolytic cleavage, lipidization, signal peptide cleavage, propeptide cleavage, phosphorylation, and such like. Peptides and peptide ligands The present invention provides peptides which are capable of binding to TLR3. A peptide capable of binding to TLR3 as provided herein may be comprised, for example, in a peptide ligand comprising said peptide ligand covalently bound to a molecular scaffold (e.g. a molecular scaffold as described in more detail herein) such that two or more peptide loops are formed on the molecular scaffold. A peptide ligand may be attached directly or indirectly (e.g. via a linker, spacer or hinge moiety) to another peptide ligand (i.e. two or more peptide ligands, which may be the same or different, may be attached together) thereby forming a complex as described in more detail herein. A peptide, peptide ligand or complex comprising multiple peptide ligands may be attached directly or indirectly (e.g. via a linker) to one or more effector groups and / or functional groups, such as one or more cytotoxic agents, radiochelators or chromophores. I n one embodiment, therefore, provided herein is a peptide ligand comprising a polypeptide having an amino acid sequence which is selected from SEQ ID NO: 1 to 366 as defined herein, or a modified derivative thereof, or a pharmaceutically acceptable salt thereof. In some embodiments, the peptide is capable of binding to TLR3. In some embodiments, the peptide is specific for TLR3. Toll-like receptors (TLRs) are a family of transmembrane proteins that play a crucial role in the innate immune system by recognizing various pathogen-associated molecular patterns (PAMPs) and initiating an immune response. One member of this family is Toll-Like Receptor 3 (TLR3; also known as CD283 (cluster of differentiation 283)), which is known for its ability to detect double-stranded RNA (dsRNA), a common viral pathogen-associated molecular pattern. TLR3 was first discovered in the late 1990s as a pattern recognition receptor involved in the recognition of viral infections. It is expressed in various immune cells, including dendritic cells, macrophages, and natural killer cells, as well as non-immune cells, such as epithelial cells. The structure of TLR3 consists of an extracellular domain with leucine-rich repeats (LRRs) responsible for ligand recognition, a transmembrane domain, and an intracellular Toll / interleukin-1 receptor (TIR) domain that initiates downstream signaling pathways upon activation. Unlike other TLRs, TLR3 does not rely on the adaptor molecule MyD88 for signaling but instead utilizes the TIR-domain-containing adaptor inducing interferon-ȕ^ ^75,)^^^ DOVR^ known as TICAM-1. Upon binding to dsRNA, TLR3 undergoes dimerization (Leonard et al (2008) PNAS 105(1), 258-263), leading to the recruitment of TRIF to the TIR domain. This triggers a signaling cascade that ultimately activates transcription factors, such as interferon regulatory factors (IRFs) and nuclear factor kappa B (NF-^%^ (Gosu et al (2019) Sci Rep 9, 3652; Bell et al (2006) PNAS 103(23), 8792-8797). These transcription factors induce the expression of type I interferons (IFNs), pro-inflammatory cytokines, and other molecules involved in antiviral defense. The activation of TLR3 and subsequent production of type I interferons and pro-inflammatory cytokines contribute to the antiviral immune response. Type I interferons are crucial for establishing an antiviral state in neighboring cells, inhibiting viral replication, and activating immune cells. Additionally, TLR3 activation can enhance the antigen-presenting capacity of dendritic cells, promoting the initiation of adaptive immune responses. TLR3 has been implicated in the immune response against a variety of viral infections, including RNA viruses such as influenza, picornaviruses, and coronaviruses. Its role in antiviral defense makes TLR3 an attractive target for the development of antiviral therapies and vaccine adjuvants. Additionally, dysregulation of TLR3 signaling has been associated with autoimmune diseases and chronic inflammatory conditions. In summary, Toll-Like Receptor 3 (TLR3) is an essential component of the innate immune system, recognizing viral double-stranded RNA and initiating immune responses. Its activation triggers the production of type I interferons and pro-inflammatory cytokines, promoting antiviral defense and shaping adaptive immune responses. The study of TLR3 provides valuable insights into host-virus interactions and has potential implications for the development of therapeutic interventions against viral infections. It will be appreciated that the therapeutic effect of an agent which binds to TLR3 will depend upon whether its binding exerts an agonistic effect or an antagonistic effect. Over the past few years, numerous studies have demonstrated the efficacy of TLR3 agonists to reinforce tumor- specific immune responses in mice and patients, especially in combination with other therapeutic approaches (Le Naour et al (2020) Oncoimmunology 9(1), 1771143). A detailed review of the link between TLR and oncology may be found in Naour and Kroemer (2023) Oncoimmunology 12(1), 2180237. In one embodiment, the peptide ligand is specific for (i.e. binds to) TLR3. The peptide ligand may be specific for (i.e. binds to) a particular epitope of TLR3, for example the soluble ectodomain of human TLR3. In some embodiments, the peptide ligand is specific for (i.e. binds to) the membrane-proximal C-terminus of TLR3. In some embodiments, the peptide ligand is specific for (i.e. binds to) the inside of the horseshoe of the TLR3 contacting one-third RI^WKH^ȕ-strands (residues 18-^^^^RI^WKH^^^^ȕ-strands of the LRR motif In some embodiments, the peptide ligand comprises a polypeptide having an amino acid sequence: C-X1-X2-X3-C-X4-X5-X6-X7-X8-X9-C (SEQ ID NO: 1) wherein each of X1to X9is independently selected from D, N, P, Y, A, I, S, T, G, Q, R, L, K, W, M, F, H, V, dA, 26DiMeTyr, 2FTyr, 3FTyr, 3tBuTyr, 4FPhe, 4tBuPhe, Aze, Cba, HyP, Cis- HyP, tBuAla, 1Nal, 2Nal, tBuGly, Aib, Pip, 5FTrp, 5MeOTrp, 6ClTrp, 6FTrp, 6MeTrp, Agb, HArg, Trp(Me), Trp(S), Cbg, His1Me, and His3Me; or a modified derivative and / or pharmaceutically acceptable salt thereof. In some embodiments, each of X1to X3is independently selected from D, N, P, Y, A, I, S, T, G, Q, R, F, dA, 26DiMeTyr, 2FTyr, 3FTyr, 4FPhe, Aze, Cba, HyP, Cis-HyP, tBuAla, tBuGly, Aib, and Pip. In some embodiments, each of X4to X9is independently selected from L, S, K, P, R, W, M, A, F, Q, Y, H, I, N, V, D, Cba, 5FTrp, 5MeOTrp, 6ClTrp, 6FTrp, 6MeTrp, Agb, HArg, Trp(Me), Trp(S), 2FTyr, 3FTyr, 3tBuTyr, 4FPhe, Cbg, His1Me, His3Me, tBuGly, 1Nal, 2Nal, 4tBuPhe, and tBuAla. In some embodiments, X1represents D, N, P, Y, 26DiMeTyr, 2FTyr, 3FTyr, or 4FPhe; X2represents A, I, N, P, S, T, Aze, Cba, Cis-HyP, tBuAla, or tBuGly; X3represents A, G, N, P, Q, R, Aib, Aze, Cis-HyP, dA, HyP, or Pip; X4represents L, S, or Cba; X5represents K, P, R, W, 5FTrp, 5MeOTrp, 6ClTrp, 6FTrp, 6MeTrp, Agb, HArg, Trp(Me), or Trp(S); X6represents M, R, or HArg; X7represents A, F, Q, Y, 2FTyr, 3FTyr, 3tBuTyr, or 4FPhe; X8represents H, I, N, V, Cbg, His1Me, His3Me, or tBuGly; and / or X9represents D, F, L, 1Nal, 2Nal, 4tBuPhe, Cba, or tBuAla. In some embodiments, X1-X2-X3is P-P-G. In some embodiments, X5is P and / or X6is R. In some embodiments, X4-X5-X6-X7-X8-X9is S-P-R-F / Y-H-L. In some embodiments, the peptide ligand comprises a polypeptide having an amino acid sequence: C-X10-X11-Y-Y-C-X12-Q-T-X13-X14-F-C (SEQ ID NO: 2) wherein each of X10to X14is independently selected from S, T, K, E, Q, R, V and H; or a modified derivative and / or pharmaceutically acceptable salt thereof. In some embodiments, X10and X11are each independently selected from S, T and K. In some embodiments, each of X12to X14is independently selected from E, Q, R, V and H. In some embodiments, X10represents S or T; X11represents K or S; X12represents E or Q; X13represents R or V; and / or X14represents H or R. In some embodiments, the peptide ligand comprises a polypeptide having an amino acid sequence: X15-X16-X17-X18-X19-X20-X21-X22-X23-X24-X25-X26-X27-X28-X29(SEQ ID NO: 3); wherein each of X16to X19and X21to X28is independently selected from A, D, H, I, L, M, N, P, S, T, W, E, Q, Y, R, V, F, R, G, K, CF3Nva, dP, HyP, Nle, Nva, TfNle, 26DiMeTyr, Cba, dL, tBuAla, Agb, Cit, dD, HArg, AlloIle, CF3Ala, HLeu, 1Nal, 2FPhe, 2MePhe, 2Nal, 3FPhe, 3MePhe, 4FPhe, 4MePhe, dE, 2FTyr, 3FTyr, 3tBuTyr, DOPA, dY, 4MeoTrp, 5FTrp, dW, Gla, Trp(S), dS, K(PYA), 2MeTrp, 4FTrp, 5MeTrp, 6FTrp, 6MeTrp, 7FTrp, 7MeTrp, dR, Trp(Me), dA, 44DFP, 4FlPro, Aze, Pip, and trans-4FlPro; X15is C or dC; X20is C or dC; and X29is C, dC, or Cystam; or a modified derivative and / or pharmaceutically acceptable salt thereof. In some embodiments, each of X16to X19is independently selected from A, D, H, I, L, M, N, P, S, T, W, E, Q, Y, R, V, CF3Nva, dP, HyP, Nle, Nva, TfNle, 26DiMeTyr, Cba, dL, tBuAla, Agb, Cit, dD, HArg, AlloIle, CF3Ala, and HLeu. In some embodiments, each of X21to X28is independently selected from A, E, F, L, Q, R, T, W, Y, V, D, H, M, Q, S, N, G, P, K, 1Nal, 2FPhe, 2MePhe, 2Nal, 3FPhe, 3MePhe, 4FPhe, 4MePhe, dE, 26DiMeTyr, 2FTyr, 3FTyr, 3tBuTyr, DOPA, dY, 4MeoTrp, 5FTrp, dW, Gla, Trp(S), dS, K(PYA), Nle, Cba, 2MeTrp, 4FTrp, 5MeTrp, 6FTrp, 6MeTrp, 7FTrp, 7MeTrp, Cit, dR, HArg, Trp(Me), Agb, dA, 44DFP, 4FlPro, Aze, dL, HyP, Pip, tBuAla, and trans-4FlPro. In some embodiments, X16represents A, D, H, I, L, M, N, P, S, T, W, CF3Nva, dP, HyP, Nle, Nva, or TfNle; X17represents E, L, N, P, Q, S, T, Y, 26DiMeTyr, Cba, dL, or tBuAla; X18represents D, E, L, P, R, T, Agb, Cba, Cit, dD, HArg, or tBuAla; X19represents A, E, I, L, M, Q, V, AlloIle, Cba, CF3Ala, dL, HLeu, Nle, or tBuAla; X21represents A, E, F, L, Q, R, T, W, Y, 1Nal, 2FPhe, 2MePhe, 2Nal, 3FPhe, 3MePhe, 4FPhe, 4MePhe, or dE; X22represents A, R, V, Y, 26DiMeTyr, 2FTyr, 3FTyr, 3tBuTyr, 4FPhe, DOPA, or dY; X23represents A, D, W, 1Nal, 2Nal, 4MeoTrp, 5FTrp, dW, Gla, or Trp(S); X24represents A, D, E, H, M, Q, S, Y, dS, K(PYA), or Nle; X25represents E, F, L, N, S, T, V, Cba, or dS; X26represents R, W, Y, 1Nal, 2FTyr, 2MeTrp, 2Nal, 3FTyr, 4FTrp, 5FTrp, 5MeTrp, 6FTrp, 6MeTrp, 7FTrp, 7MeTrp, Cit, dR, HArg, or Trp(Me); X27represents G, R, S, Agb, Cit, dA, dE, or HArg; and / or X28represents L, P, 44DFP, 4FlPro, Aze, Cba, dL, HyP, Pip, tBuAla, or trans-4FlPro; wherein X15represents C or dC; X20represents C or dC; and X29represents C, dC, or Cysam. In some embodiments, X16-X17-X18-X19is P-L-D-L. In some embodiments, X16-X17-X18-X19is M / CF3Nva-Y-R-A. In some embodiments, X22is Y, and / or X23is W or 5FTrp. In some embodiments, X21-X22-X23- X24-X25-X26-X27-X28is E-Y-W / 5FTrp-S-S / V-R-G-L. In some embodiments, X26is W or 1 Nal, and / or X27is R, and / or X28is P. In some embodiments, X21-X22-X23-X24-X25-X26-X27-X28is W / F- V / Y-A / D-E / D-E-W / 1Nal-R-P. In some embodiments, the peptide ligand comprises a polypeptide having an amino acid sequence: C-Q-P-T-X30-X31-C-X32-X33-X34-X35-X36-X37-C (SEQ ID NO: 4) wherein each of X30to X37is independently selected from P, E, Q, R, F, Y, N, S, T, W, A, Cis-HyP, HyP, Pip, Aze, 2FTyr, 2Nal, 3FTyr, 4FPhe, 4tBuPhe, Dap, 1Nal, 4MeoTrp, 5FTrp, 5MeoTrp, 6ClTrp, 6FTrp, AzaTrp, and Trp(S); or a modified derivative and / or pharmaceutically acceptable salt thereof. In some embodiments, X30and X31are each independently selected from P, E, Q, R, Cis-HyP, HyP, and Pip. In some embodiments, each of X32 to X37 is independently selected from P, F, Y, N, S, T, W, A, Aze, Cis-HyP, HyP, 2FTyr, 2Nal, 3FTyr, 4FPhe, 4tBuPhe, Dap, 1Nal, 4MeoTrp, 5FTrp, 5MeoTrp, 6ClTrp, 6FTrp, AzaTrp, Trp(S), and Pip. In some embodiments, X30represents P, Cis-HyP, HyP, or Pip; X31represents E, Q, or R; X32represents P, Aze, Cis-HyP, or HyP; X33represents F, Y, 2FTyr, 2Nal, 3FTyr, 4FPhe, or 4tBuPhe; X34represents N, S, or Dap; X35represents T or Dap; X36represents W, 1Nal, 2Nal, 4MeoTrp, 5FTrp, 5MeoTrp, 6ClTrp, 6FTrp, AzaTrp, or Trp(S); and / or X37represents P, Aze, Cis-HyP, HyP, or Pip. In some embodiments, X30is P. In some embodiments, X30-X31is P-R / Q. In some embodiments, X36is W. In some embodiments, X32-X33-X34-X35-X36-X37is P-F / Y-S-T-W-P. In some embodiments, the peptide ligand comprises a polypeptide having an amino acid sequence: C-Y-Y-X38-X39-X40-Y-A-C-L-D-C (SEQ ID NO: 5) wherein each of X38to X40is independently selected from E, P, D, N, W and Y; or a modified derivative and / or pharmaceutically acceptable salt thereof. In some embodiments, X38represents E or P; X39represents D or N; and / or X40represents W or Y. In some embodiments, the peptide ligand comprises a polypeptide having an amino acid sequence: X41-X42-X43-X44-X45-X46-X47-X48-X49-C-X50-X51-X52-X53-X54(SEQ ID NO: 6) wherein each of X42to X53is independently selected from A, D, E, G, K, N, P, S, T, V, Y, H, M, Q, F, I, W, R, L, 3HyV, Aib, CF3Ala, dA, Dap, dK(PYA), dS, HSer, K(PYA), 4FlPro, Cis- Hyp, HyP, trans-4FlPro, 1Nal, 26DiMeTyr, 2FTyr, 2Nal, 3FTyr, 4FPhe, DOPA, 2FPhe, 4CF3Phe, Cba, CF3Nva, Nle, Nva, tBuAla, TfNle, 2MeTrp, 4FTrp, 4MeTrp, 5FTrp, 5MeTrp, 6FTrp, 6MeTrp, 7FTrp, 7MeTrp, AzaTrp, Agb, HArg, Orn, 5MeoTrp, C5g, Cbg, tBuGly, Trp(S), Arg(Me), PG, Cit, R-aMeLys(PYA), S-aMeLys(PYA), and EPA; X41is C or dC; X54is C, dC, or Cystam,; or a modified derivative and / or pharmaceutically acceptable salt thereof. In some embodiments, each of X42to X49is independently selected from A, D, E, G, K, N, P, S, T, V, Y, H, M, Q, F, I, W, R, L, 3HyV, Aib, CF3Ala, dA, Dap, dK(PYA), dS, HSer, K(PYA), 4FlPro, Cis-Hyp, HyP, trans-4FlPro, 1Nal, 26DiMeTyr, 2FTyr, 2Nal, 3FTyr, 4FPhe, DOPA, 2FPhe, 4CF3Phe, Cba, CF3Nva, Nle, Nva, tBuAla, TfNle, 2MeTrp, 4FTrp, 4MeTrp, 5FTrp, 5MeTrp, 6FTrp, 6MeTrp, 7FTrp, 7MeTrp, AzaTrp, Agb, HArg, Orn, 5MeoTrp, C5g, Cbg, tBuGly, and Trp(S). In some embodiments, each of X50to X53is independently selected from E, M, Q, R, S, T, A, K, G, L, N, P, Q, D, I, V, Arg(Me), Dap, HArg, PG, 3HyV, Cit, Orn, Cba, dA, dK(PYA), K(PYA), Nle, Nva, R-aMeLys(PYA), S-aMeLys(PYA), tBuAla, EPA, and tBuGly. In some embodiments, X42represents A, D, E, G, K, N, P, S, T, V, Y, 3HyV, Aib, CF3Ala, dA, Dap, dK(PYA), dS, HSer, or K(PYA); X43represents N, T, or 3HyV; X44represents D, E, P, 4FlPro, Cis-Hyp, HyP, or trans-4FlPro; X45represents A, H, M, Q, S, V, Y, 1Nal, 26DiMeTyr, 2FTyr, 2Nal, 3FTyr, 4FPhe, DOPA, or HSer; X46represents A, E, F, I, M, V, 2FPhe, 4CF3Phe, Cba, CF3Nva, Nle, Nva, tBuAla, or TfNle; X47represents A, E, S, T, W, 1Nal, 2MeTrp, 4FTrp, 4MeTrp, 5FTrp, 5MeTrp, 6FTrp, 6MeTrp, 7FTrp, 7MeTrp, AzaTrp, CF3Ala, or Dap; X48represents K, R, Y, 2FTyr, 3FTyr, Agb, DOPA, HArg, or Orn; X49represents A, D, L, V, W, 1Nal, 2Nal, 3HyV, 4FTrp, 5FTrp, 5MeoTrp, 6FTrp, AzaTrp, C5g, Cbg, tBuGly, or Trp(S); X50represents E, M, Q, R, S, T, Arg(Me), Dap, HArg, or PG; X51represents A, E, K, M, R, S, T, 3HyV, Cit, HArg, or Orn; X52represents A, G, L, M, N, P, Q, Cba, dA, dK(PYA), K(PYA), Nle, Nva, R-aMeLys(PYA), S-aMeLys(PYA), or tBuAla; X53represents D, I, L, M, V, EPA, Nle, Nva, or tBuGly; wherein X41represents C or dC and X54represents C, dC, or Cysam. In some embodiments, X48is Y and / or X49is W and / or 5FTrp. In some embodiments, X42-X43-X44-X45-X46-X47-X48-X49is N / D-N-P / E-V-M / I-T-Y-W / 5FTrp. In some embodiments, X47is W, and / or X48is K, and / or X49is V. In some embodiments, X42- X43-X44-X45-X46-X47-X48-X49is T / S-T-D-M / Y-M / Nle-W-K-V. In some embodiments, X50-X51-X52- X53is T / Q-K / R-G-I. In some embodiments, X50is R. In some embodiments, X50-X51-X52-X53is R-T-L-D. In one embodiment, the peptide ligand of C-X1-X2-X3-C-X4-X5-X6-X7-X8-X9-C (SEQ ID NO: 1) comprises an amino acid sequence selected from: CDI ACLKM YNFC (SEQ ID NO: 7); CDI GCLR MYNFC (SEQ ID NO: 8); CD[tBuAla]G CLRMY NFC (SEQ ID NO: 9); CD[tBuGly]G CLRMY NFC (SEQ ID NO: 10); CD[Cba]G CLRM YNFC (SEQ ID NO: 11); CDI [dA]CLRM YNFC (SEQ ID NO: 12); CDI [Aib]CLR MYNFC (SEQ ID NO: 13); CDI GC[Cba]R MYNFC (SEQ ID NO: 14): CDI GCL[HArg]M YNFC (SEQ ID NO: 15): CDI GCL[Agb]M YNFC (SEQ ID NO: 16); CDI GCLR MYN[1Nal] C (SEQ ID NO: 17); CDI GCLR MYN[2Nal] C (SEQ ID NO: 18); CDI GCLR MYN[4tBuPhe]C (SEQ ID NO: 19); CDI QCLR MYNFC (SEQ ID NO: 20); CNI QCLR MYNFC (SEQ ID NO: 21); CDI RCLRM YNFC (SEQ ID NO: 22); CDI NCLRM YNFC (SEQ ID NO: 23); CPPG CSPRFH LC (SEQ ID NO: 24); CPPG CSPRY HLC (SEQ ID NO: 25; herein referred to as BCY21542 when complexed with a derivative of TATB which has the following structure: wherein * denotes the point of attachment of the three cysteine residues); CP[Cis-HyP]G CSPRY HLC (SEQ ID NO: 26); CP[Aze]G CSPRYH LC (SEQ ID NO: 27); CPPG CSP[HArg]YHLC (SEQ ID NO: 28); CPPG CSPR[4FPhe]H LC (SEQ ID NO: 29); CPPG CSPR[3tBuTyr]H LC (SEQ ID NO: 30): CPPG CSPR[3FTyr] HLC (SEQ ID NO: 31); CPPG CSPR[2FTyr] HLC (SEQ ID NO: 32); CPPG CSPRY [His1Me]LC (SEQ ID NO: 33); CPPG CSPRY [His3Me]LC (SEQ ID NO: 34); CPPG CSPRY H[tBuAla]C (SEQ ID NO: 35); CPPG CSPRY H[Cba]C (SEQ ID NO: 36); CPPG CSPRY NLC (SEQ ID NO: 37); CYN PCLWR QVDC (SEQ ID NO: 38; herein referred to as BCY21497 when complexed with a tri-substituted 2,4,6-tris(bromomethyl)-s-triazine derivative of TBMT having the following structure: wherein * denotes the point of attachment of the three cysteine residues); CYAP CLWR QVDC (SEQ ID NO: 39); CYN PCLWR AVDC (SEQ ID NO: 40); C[4FPhe]NP CLWRQ VDC (SEQ ID NO: 41); C[26DiMeTyr]N PCLWR QVDC (SEQ ID NO: 42); C[3FTyr]N PCLWRQVDC (SEQ ID NO: 43); C[2FTyr]N PCLWRQVDC (SEQ ID NO: 44); CYN [HyP]CLWR QVDC (SEQ ID NO: 45); CYN [Cis-HyP]CLWRQ VDC (SEQ ID NO: 46); CYN [Aze]C LWRQ VDC (SEQ ID NO: 47); CYN [Pip]CLWRQVD C (SEQ ID NO: 48); CYN PC[Cba]WRQVDC (SEQ ID NO: 49); CYN PCL[6MeTrp]RQVDC (SEQ ID NO: 50); CYN PCL[6FTrp]RQ VDC (SEQ ID NO: 51); CYN PCL[5FTrp]RQ VDC (SEQ ID NO: 52); CYN PCL[6ClTrp]RQV DC (SEQ ID NO: 53); CYN PCL[5MeoTrp]RQVDC (SEQ ID NO: 54); CYN PCL[Trp(S)]RQVDC (SEQ ID NO: 55); CYN PCL[Trp(Me)]RQVD C (SEQ ID NO: 56); CYN PCLWR Q[tBuGly]DC (SEQ ID NO: 57); CYN PCLWR Q[Cbg]DC (SEQ ID NO: 58); CYN PCLWR QID C (SEQ ID NO: 59); CYSP CLWR QVDC (SEQ ID NO: 60); and CYTPC LWRQ VDC (SEQ ID NO: 61). In one embodiment, the peptide ligand of C-X10-X11-Y-Y-C-X12-Q-T-X13-X14-F-C (SEQ ID NO: 2) comprises an amino acid sequence selected from: CTSYY CEQTRH FC (SEQ ID NO: 62); CTKYY CEQTRH FC (SEQ ID NO: 63); and CSKY YCQQ TVRFC (SEQ ID NO: 64). In one embodiment, the peptide ligand of X15-X16-X17-X18-X19-X20-X21-X22-X23-X24-X25-X26-X27- X28-X29(SEQ ID NO: 3) comprises an amino acid sequence selected from: CTNE VCTYWYNRGLC (SEQ ID NO: 65); CAN EVCEYWYNRG LC (SEQ ID NO: 66); CPLD LCEYWSFRGLC (SEQ ID NO: 67); CTNE VCRYWYNRG LC (SEQ ID NO: 68); CDS PVCEYWSFRGLC (SEQ ID NO: 69); CHN EVCEYWSFRG LC (SEQ ID NO: 70); CSN EVCEYWSFRGLC (SEQ ID NO: 71); CSN PVCEYWSFRGLC (SEQ ID NO: 72); CNN PVCEYWSFRG LC (SEQ ID NO: 73); CDN EVCEYWSFRG LC (SEQ ID NO: 74); CTSEV CEYWSFRGLC (SEQ ID NO: 75); CSTLVC QRDQ LYSLC (SEQ ID NO: 76); CHN EVCLYWYNRG LC (SEQ ID NO: 77); CWNPVCE YWYN RGLC (SEQ ID NO: 78); CATLQ CQRD MLYGLC (SEQ ID NO: 79); CSTLVC QRDQ LYGLC (SEQ ID NO: 80); CST[tBuAla]VC QRDQ LYGLC (SEQ ID NO: 81); CST[Cba]V CQRDQ LYGLC (SEQ ID NO: 82); CSTL[tBuAla]C QRDQ LYGLC (SEQ ID NO: 83); CSTLVC QRD[Nle] LYGLC (SEQ ID NO: 84); CSTLVC QRDQ [Cba]YGLC (SEQ ID NO: 85); CSTLVC QRDQ LY[dA]LC (SEQ ID NO: 86); CSTLVC QRDQ LYG[tBuAla]C (SEQ ID NO: 87); CSTLVC QRDQ LYG[Cba]C (SEQ ID NO: 88); CST[tBuAla]VC QRDQ LY[dA]LC (SEQ ID NO: 89); CNP LICQ RDQLYG LC (SEQ ID NO: 90); CI SLACQR DQLYG LC (SEQ ID NO: 91); CSTLEC QRDQ LYGLC (SEQ ID NO: 92); CNTLV CQRDQ LYGLC (SEQ ID NO: 93); CTQLM CQR DQLYGLC (SEQ ID NO: 94); CTELM CQRD QLYGLC (SEQ ID NO: 95); CTE[tBuAla]M CQRD QLY[dA]LC (SEQ ID NO: 96); CTELM CQRD QLY[dA]LC (SEQ ID NO: 97); CTE[tBuAla]M CQRD QLYGLC (SEQ ID NO: 98); CTELAC QRDQ LYGLC (SEQ ID NO: 99); CTEL[Nle] CQR DQLYGLC (SEQ ID NO: 100); CTEL[HLeu]C QRDQ LYGLC (SEQ ID NO: 101); CTELM CQR[Gla]QLYG LC (SEQ ID NO: 102); CTELM CQRD QL[3FTyr]GLC (SEQ ID NO: 103); CTELM CQRD QL[2FTyr]GLC (SEQ ID NO: 104); CAN TVCAYWETRGLC (SEQ ID NO: 105); CAN TVCAY[5FTrp] ETRGLC (SEQ ID NO: 106); CPLD LCEYWSVRGLC (SEQ ID NO: 107); CPLD LCEYWSSRGLC (SEQ ID NO: 108); C[HyP]LDLC EYWS SRGLC (SEQ ID NO: 109); CP[tBuAla]D LCEYWSSRGLC (SEQ ID NO: 110); CP[Cba]D LCEYWSSRGLC (SEQ ID NO: 111); CPLD [AlloIle]CEY WSSR GLC (SEQ ID NO: 112); CPLD [tBuAla]CEYWSSRGLC (SEQ ID NO: 113); CPLD [Cba]CEYWSSRGLC (SEQ ID NO: 114); CPLD VCEYWSSRGLC (SEQ ID NO: 115); CPLD LCE[4FPhe]WS SRGLC (SEQ ID NO: 116); CPLD LCEY[2Nal]S SRGLC (SEQ ID NO: 117); CPLD LCEY[1Nal]S SRGLC (SEQ ID NO: 118); CPLD LCEY[5FTrp]S SRGLC (SEQ ID NO: 119); CPLD LCEY[4MeoTrp]SSRG LC (SEQ ID NO: 120); CPLD LCEY[Trp(S)]SSRGLC (SEQ ID NO: 121); CPLD LCEYWSS[HArg]GLC (SEQ ID NO: 122); CPLD LCEYWSS[Cit]GLC (SEQ ID NO: 123); CPLD LCEYWSSR[dA]LC (SEQ ID NO: 124); CPLD LCEYWSSRG[tBuAla]C (SEQ ID NO: 125); CPLD LCEYWSSRG[Cba]C (SEQ ID NO: 126); [dC][dP][dL][dD][dL][dC][dE][dY][dW] [dS][dS][dR]G[dL][dC] (SEQ ID NO: 127); CP[Cba]D LCEY[5FTrp] SSRGLC (SEQ ID NO: 128); CPLD LCEYW[K(PYA)]SRG LC (SEQ ID NO: 129, herein referred to as BCY21632 when complexed with a derivative of TATA which has the following structure: wherein * denotes the point of attachment of the three cysteine residues); CPLD LCEYW[K(PYA)]SRG L[Cysam] (SEQ ID NO: 130, herein referred to as BCY21637 when complexed with a derivative of TATA which has the following structure: wherein * denotes the point of attachment of the three cysteine residues); CPLD LCEY[5FTrp]E SRGLC (SEQ ID NO: 131); CPN DLCEY[5FTrp] SSRGLC (SEQ ID NO: 132); CPLD LCEY[5FTrp]S SR[dA]LC (SEQ ID NO: 133); CPLD LCEY[5FTrp]S SR[dE]LC (SEQ ID NO: 134); CPLD [tBuAla]CEY[5FTrp]S S[HArg][dA]LC (SEQ ID NO: 135); CP[Cba]D LCEY[5FTrp] SS[HArg][dA]LC (SEQ ID NO: 136); CPN DLCEYWSVRG LC (SEQ ID NO: 137); CI TLQCARD MLYGLC (SEQ ID NO: 138); CSTLQ CERDM LYGLC (SEQ ID NO: 139); CI SLACARD MLYGLC (SEQ ID NO: 140); CSTLQ CQRD MLYGLC (SEQ ID NO: 141); CM YRACWVAEEWRPC (SEQ ID NO: 142); CM YRACYY DHEWRPC (SEQ ID NO: 143); CM YRACFYD DEWR PC (SEQ ID NO: 144); CM YRACAY DDEWRPC (SEQ ID NO: 145); CM YRACFAD DEWR PC (SEQ ID NO: 146); CM YRACFYA DEWR PC (SEQ ID NO: 147); CM YRACFYD AEWR PC (SEQ ID NO: 148); C[Nle] YRACFY DDEWRPC (SEQ ID NO: 149); C[Nva]YRA CFYDDE WRPC (SEQ ID NO: 150); C[TfNle]YRA CFYDDE WRPC (SEQ ID NO: 151); C[CF3Nva]YR ACFYDD EWRP C (SEQ ID NO: 152); CM [26DiMeTyr]RACFYD DEWR PC (SEQ ID NO: 153); CM Y[HArg]A CFYDDE WRPC (SEQ ID NO: 154); CM Y[Agb]ACFYDD EWRP C (SEQ ID NO: 155); CM Y[Cit]ACFYDD EWRP C (SEQ ID NO: 156); CM YR[CF3Ala]CFYDDEWRPC (SEQ ID NO: 157); CM YRAC[1Nal] YDDEWRPC (SEQ ID NO: 158); CM YRAC[2Nal] YDDEWRPC (SEQ ID NO: 159); CM YRAC[4MePhe] YDDEWRPC (SEQ ID NO: 160); CM YRAC[3MePhe] YDDEWRPC (SEQ ID NO: 161); CM YRAC[2MePhe] YDDEWRPC (SEQ ID NO: 162); CM YRAC[4FPhe]YD DEWR PC (SEQ ID NO: 163); CM YRAC[3FPhe]YD DEWR PC (SEQ ID NO: 164); CM YRAC[2FPhe]YD DEWR PC (SEQ ID NO: 165); CM YRACF[4FPhe]DD EWR PC (SEQ ID NO: 166); CM YRACF[3tBuTyr]DD EWRP C (SEQ ID NO: 167); CM YRACF[26DiMeTyr]D DEWR PC (SEQ ID NO: 168); CM YRACF[3FTyr] DDEWRPC (SEQ ID NO: 169); CM YRACF[2FTyr] DDEWRPC (SEQ ID NO: 170); CM YRACF[DOPA]DDE WRPC (SEQ ID NO: 171); CM YRACFYD DE[1Nal]R PC (SEQ ID NO: 172); CM YRACFYD DE[2Nal]R PC (SEQ ID NO: 173); CM YRACFYD DE[4FTrp]R PC (SEQ ID NO: 174); CM YRACFYD DE[5FTrp]R PC (SEQ ID NO: 175); CM YRACFYD DE[6FTrp]R PC (SEQ ID NO: 176); CM YRACFYD DE[7FTrp]R PC (SEQ ID NO: 177); CM YRACFYD DE[Trp(Me)]RPC (SEQ ID NO: 178); CM YRACFYD DE[2MeTrp]RPC (SEQ ID NO: 179); CM YRACFYD DE[5MeTrp]RPC (SEQ ID NO: 180); CM YRACFYD DE[6MeTrp]RPC (SEQ ID NO: 181); CM YRACFYD DE[7MeTrp]RPC (SEQ ID NO: 182); CM YRACFYD DEW[HArg]PC (SEQ ID NO: 183); CM YRACFYD DEW[Agb]P C (SEQ ID NO: 184); CM YRACFYD DEW[Cit]P C (SEQ ID NO: 185); CM YRACFYD DEWR [HyP]C (SEQ ID NO: 186); CM YRACFYD DEWR [Aze]C (SEQ ID NO: 187); CM YRACFYD DEWR [Pip]C (SEQ ID NO: 188); CM YRACFYD DEWR [44DFP]C (SEQ ID NO: 189); CM YRACFYD DEWR [4FlPro]C (SEQ ID NO: 190); CM YRACFYD DEWR [trans-4FlPro]C (SEQ ID NO: 191); C[CF3Nva]YR ACFYDD E[1Nal]RP C (SEQ ID NO: 192); C[CF3Nva]YR AC[4MePhe]Y DDE[1Nal] RPC (SEQ ID NO: 193); CLYR ACFYDDE WRPC (SEQ ID NO: 194); CLYR AC[4MePhe]YD DE[1Nal]R PC (SEQ ID NO: 195); CHY RACFYDD EWRP C (SEQ ID NO: 196); In one embodiment, the peptide ligand of C-Q-P-T-X30-X31-C-X32-X33-X34-X35-X36-X37-C (SEQ ID NO: 4) comprises an amino acid sequence selected from: CQ PTPRCPFSTWPC (herein referred to as SEQ ID NO: 197); CQ PTPQCPY STWPC (herein referred to as SEQ ID NO: 198, herein referred to as BCY20723 when complexed with a derivative of TATB which has the following structure: wherein * denotes the point of attachment of the three cysteine residues); CQ PT[HyP]QCPY STWPC (herein referred to as SEQ ID NO: 199); CQ PT[Cis-HyP]QCPYS TWPC (herein referred to as SEQ ID NO: 200); CQ PT[Pip]QC PYSTWPC (herein referred to as SEQ ID NO: 201); CQ PTPECPYS TWPC (herein referred to as SEQ ID NO: 202); CQ PTPQC[HyP]Y STWPC (herein referred to as SEQ ID NO: 203); CQ PTPQC[Cis-HyP]YS TWPC (herein referred to as SEQ ID NO: 204); CQ PTPQC[Aze]YSTWPC (herein referred to as SEQ ID NO: 205); CQ PTPQCP[2Nal] STWPC (herein referred to as SEQ ID NO: 206); CQ PTPQCP[4tBuPhe]STWPC (herein referred to as SEQ ID NO: 207); CQ PTPQCP[4FPhe]S TWPC (herein referred to as SEQ ID NO: 208); CQ PTPQCP[3FTyr] STWP C (herein referred to as SEQ ID NO: 209); CQ PTPQCP[2FTyr] STWP C (herein referred to as SEQ ID NO: 210); CQ PTPQCPY [Dap]TWPC (herein referred to as SEQ ID NO: 211); CQ PTPQCPY S[Dap]WPC (herein referred to as SEQ ID NO: 212); CQ PTPQCPY ST[2Nal]PC (herein referred to as SEQ ID NO: 213); CQ PTPQCPY ST[1Nal]PC (herein referred to as SEQ ID NO: 214); CQ PTPQCPY ST[6FTrp]PC (herein referred to as SEQ ID NO: 215); CQ PTPQCPY ST[5FTrp]PC (herein referred to as SEQ ID NO: 216); CQ PTPQCPY ST[6ClTrp]PC (herein referred to as SEQ ID NO: 217); CQ PTPQCPY ST[4MeoTrp]P C (herein referred to as SEQ ID NO: 218); CQ PTPQCPY ST[5MeoTrp]P C (herein referred to as SEQ ID NO: 219); CQ PTPQCPY ST[Trp(S)]PC (herein referred to as SEQ ID NO: 220); CQ PTPQCPY ST[AzaTrp]PC (herein referred to as SEQ ID NO: 221); CQ PTPQCPY STW[HyP]C (herein referred to as SEQ ID NO: 222); CQ PTPQCPY STW[Cis-HyP]C (herein referred to as SEQ ID NO: 223); CQ PTPQCPY STW[Aze]C (herein referred to as SEQ ID NO: 224); CQ PTPQCPY STW[Pip] C (herein referred to as SEQ ID NO: 225); and CQ PTPECPYN TWPC (herein referred to as SEQ ID NO: 226). In one embodiment, the peptide ligand of C-Y-Y-X38-X39-X40-Y-A-C-L-D-C (SEQ ID NO: 5) comprises an amino acid sequence selected from: CYYP DYYACLD C (herein referred to as SEQ ID NO: 227); CYYE NYYACLD C (herein referred to as SEQ ID NO: 228); and CYYP DWYA CLDC (herein referred to as SEQ ID NO: 229). In one embodiment, the peptide ligand of X41-X42-X43-X44-X45-X46-X47-X48-X49-C-X50-X51-X52- X53-X54(SEQ ID NO: 6) comprises an amino acid sequence selected from: CNN PVMTYWCTKG IC (herein referred to as SEQ ID NO: 230); CNN PVMTYWCEKG IC (herein referred to as SEQ ID NO: 231); CDN EVITYWCTKG IC (herein referred to as SEQ ID NO: 232); CDN EV[tBuAla]TYWCTKGI C (herein referred to as SEQ ID NO: 233); CDN EVFTYWCTKGI C (herein referred to as SEQ ID NO: 234); CDN EV[Cba]TYWCTKGI C (herein referred to as SEQ ID NO: 235); CDN EVITY[2Nal] CTKG IC (herein referred to as SEQ ID NO: 236); CDN EVITY[1Nal] CTKG IC (herein referred to as SEQ ID NO: 237); CDN EVITYWCT[Orn]GI C (herein referred to as SEQ ID NO: 238); CDN EVITYWCT[HArg]GI C (herein referred to as SEQ ID NO: 239); CDN EVITYWCTK[dA]I C (herein referred to as SEQ ID NO: 240); CDN EVITYWCTKG [tBuGly]C (herein referred to as SEQ ID NO: 241); CDN EVIT[DOPA]WCTKGI C (herein referred to as SEQ ID NO: 242); CDN PVFTYWCTKGI C (herein referred to as SEQ ID NO: 243); CNN PVMAY WCTKG IC (herein referred to as SEQ ID NO: 244); CPN PVITYWCTKG IC (herein referred to as SEQ ID NO: 245); CDN EVITYWCQ MGVC (herein referred to as SEQ ID NO: 246); CDN EVITYWCQ RGVC (herein referred to as SEQ ID NO: 247); CDN EVITYWCM RGI C (herein referred to as SEQ ID NO: 248); CDN EVITYWCQ RGIC (herein referred to as SEQ ID NO: 249); CDN EVITY[6FTrp] CQR GIC (herein referred to as SEQ ID NO: 250); CDN EVITY[5FTrp] CQR GIC (herein referred to as SEQ ID NO: 251); CDN EVITY[5MeoTrp]CQ RGI C (herein referred to as SEQ ID NO: 252); CDN EVITY[Trp(S)]CQ RGI C (herein referred to as SEQ ID NO: 253); CDN EVITY[AzaTrp] CQR GIC (herein referred to as SEQ ID NO: 254); CDN EVITYWCQ [HArg]G IC (herein referred to as SEQ ID NO: 255); CDN EVITYWCQ [Cit]G IC (herein referred to as SEQ ID NO: 256); CDN EVFEYWCTKGI C (herein referred to as SEQ ID NO: 257); CDN EVITYWCER GIC (herein referred to as SEQ ID NO: 258); CDN EVITYWCEM GIC (herein referred to as SEQ ID NO: 259); CSN PVFAYWCSRQM C (herein referred to as SEQ ID NO: 260); CSN PVFAYWCERGI C (herein referred to as SEQ ID NO: 261, herein referred to as BCY21615 when complexed with a tri-substituted 2,4,6-tris(bromomethyl)-s-triazine derivative of TBMT having the following structure: wherein * denotes the point of attachment of the three cysteine residues); CSN PVFAYWCER[K(PYA)]IC (herein referred to as SEQ ID NO: 262); CSN PVFAYWCER[dK(PYA)]IC (herein referred to as SEQ ID NO: 263); CSN PVFAYWCER[S-aMeLys(PYA)]I C (herein referred to as SEQ ID NO: 264); CSN PVFAYWCER[R-aMeLys(PYA)]I C (herein referred to as SEQ ID NO: 265); C[K(PYA)]NPVFAY WCER GIC (herein referred to as SEQ ID NO: 266); CSN PVFAY[5FTrp] CERGI C (herein referred to as SEQ ID NO: 267); CSN PVFAYWCERGI [Cysam] (herein referred to as SEQ ID NO: 268, herein referred to as BCY21623 when complexed with a tri-substituted 2,4,6-tris(bromomethyl)-s-triazine derivative of TBMT having the following structure: wherein * denotes the point of attachment of the three cysteine residues); C[K(PYA)]NPVFAY WCER GI[Cysam] (herein referred to as SEQ ID NO: 269); CSN PVFAYWC[Dap]RGI C (herein referred to as SEQ ID NO: 270); CKN PVFAYWC[PG]RG IC (herein referred to as SEQ ID NO: 271); CEN PVFAYWCERGI C (herein referred to as SEQ ID NO: 272); C[dA]NP VFAYWCERGI C (herein referred to as SEQ ID NO: 273); CG NPVFAYWCERG IC (herein referred to as SEQ ID NO: 274); C[Aib] NPVFAYWCERG IC (herein referred to as SEQ ID NO: 275); CSN [trans-4FlPro]VFAYWCERG IC (herein referred to as SEQ ID NO: 276); CSN [4FlPro]V FAYWC ERGI C (herein referred to as SEQ ID NO: 277); CSN [HyP]VFAYWCERGI C (herein referred to as SEQ ID NO: 278); CSN [Cis-HyP]VFAYWCERGI C (herein referred to as SEQ ID NO: 279); CSN P[HSer]FA YWCE RGI C (herein referred to as SEQ ID NO: 280); CSN PV[2FPhe]AYWCERG IC (herein referred to as SEQ ID NO: 281); CSN PV[4CF3Phe]AYWCERG IC (herein referred to as SEQ ID NO: 282); CSN PVFSYWCERGI C (herein referred to as SEQ ID NO: 283); CSN PVF[Dap]YWCERGI C (herein referred to as SEQ ID NO: 284); CSN PVF[CF3Ala]Y WCER GIC (herein referred to as SEQ ID NO: 285); CSN PVFA[2FTyr]WCERG IC (herein referred to as SEQ ID NO: 286); CSN PVFA[3FTyr]WCERG IC (herein referred to as SEQ ID NO: 287); CSN PVFAY[4FTrp] CERGI C (herein referred to as SEQ ID NO: 288); CSN PVFAYWCE[Cit]GI C (herein referred to as SEQ ID NO: 289); CSN PVFAYWCER[dA]I C (herein referred to as SEQ ID NO: 290); CSN PVFAYWCERG[Nva]C (herein referred to as SEQ ID NO: 291); CSN PVFAYWCERG[Nle] C (herein referred to as SEQ ID NO: 292); CSN PVFAYWCERG[EPA] C (herein referred to as SEQ ID NO: 293); CSN PVFAYWCERG[tBuGly] C (herein referred to as SEQ ID NO: 294); CSN [4FlPro]V FAY[5FTrp]C ERG[EPA] C (herein referred to as SEQ ID NO: 295); C[Aib] N[4FlPro]VFAY[5FTrp] CERG[EPA] C (herein referred to as SEQ ID NO: 296); C[dS]N[4FlPro]V FAY[5FTrp]CE RG[EPA]C (herein referred to as SEQ ID NO: 297); C[K(PYA)]N[4FlPro]VFAY[5FTrp] CERG [EPA]C (herein referred to as SEQ ID NO: 298); C[dK(PYA)]N[4FlPro]VFAY[5FTrp] CERG [EPA]C (herein referred to as SEQ ID NO: 299); [dC]SN[4FlPro]V FAY[5FTrp]CE RG[EPA]C (herein referred to as SEQ ID NO: 300); CSN [4FlPro]V FAY[5FTrp]C ERG[EPA] [dC] (herein referred to as SEQ ID NO: 301); [dC]SN[4FlPro]V FAY[5FTrp]CE RG[EPA][dC] (herein referred to as SEQ ID NO: 302); CSN PVFAYWCSRNLC (herein referred to as SEQ ID NO: 303); CSN PVFAYWCSRGLC (herein referred to as SEQ ID NO: 304); CTTDM MWKVCRTLD C (herein referred to as SEQ ID NO: 305); CATD HMWKVCRTLDC (herein referred to as SEQ ID NO: 306); CKTD AMWKVCRTLDC (herein referred to as SEQ ID NO: 307); CSTD QMWKVCRTLD C (herein referred to as SEQ ID NO: 308); CSTD YMWKVCRTLDC (herein referred to as SEQ ID NO: 309, herein referred to as BCY23141 when complexed with a tri-substituted 2,4,6-tris(bromomethyl)-s-triazine derivative of TBMT having the following structure: wherein * denotes the point of attachment of the three cysteine residues); CSTD Y[Nle]WKVCRTLD C (herein referred to as SEQ ID NO: 310); CATD YMWKVCRTLDC (herein referred to as SEQ ID NO: 311); CSTD AMWKVCRTLDC (herein referred to as SEQ ID NO: 312); CSTD YAWKV CRTLDC (herein referred to as SEQ ID NO: 313); CSTD YMWKACRTLDC (herein referred to as SEQ ID NO: 314); CSTD YMWKVCRALD C (herein referred to as SEQ ID NO: 315); CSTD YMWKVCRTAD C (herein referred to as SEQ ID NO: 316); C[CF3Ala]TDYMWKVC RTLDC (herein referred to as SEQ ID NO: 317); C[HSer]TDYM WKVC RTLDC (herein referred to as SEQ ID NO: 318); CTTDY MWK VCRTLDC (herein referred to as SEQ ID NO: 319); C[3HyV]TDY MWKVCRTLDC (herein referred to as SEQ ID NO: 320); CS[3HyV]D YMWKVCRTLD C (herein referred to as SEQ ID NO: 321); C[Dap]TDY MWKVCRTLDC (herein referred to as SEQ ID NO: 322); CSTD [4FPhe]MWK VCRTLDC (herein referred to as SEQ ID NO: 323); CSTD [1Nal]MWKVCR TLDC (herein referred to as SEQ ID NO: 324); CSTD [2Nal]MWKVCR TLDC (herein referred to as SEQ ID NO: 325); CSTD [26DiMeTyr]MWKVCRTLDC (herein referred to as SEQ ID NO: 326); CSTD [3FTyr]MWKVCRTLD C (herein referred to as SEQ ID NO: 327); CSTD [2FTyr]MWKVCRTLD C (herein referred to as SEQ ID NO: 328); CSTD [DOPA]M WKVC RTLDC (herein referred to as SEQ ID NO: 329); CSTD Y[Nva]WKVC RTLDC (herein referred to as SEQ ID NO: 330); CSTD Y[TfNle]WKVC RTLDC (herein referred to as SEQ ID NO: 331); CSTD YEWKV CRTLDC (herein referred to as SEQ ID NO: 332); CSTD Y[CF3Nva]WKV CRTLDC (herein referred to as SEQ ID NO: 333); CSTD YM[1Nal] KVCRTLDC (herein referred to as SEQ ID NO: 334); CSTD YM[4FTrp]K VCRTLDC (herein referred to as SEQ ID NO: 335); CSTD YM[5FTrp]K VCRTLDC (herein referred to as SEQ ID NO: 336); CSTD YM[6FTrp]K VCRTLDC (herein referred to as SEQ ID NO: 337); CSTD YM[7FTrp]K VCRTLDC (herein referred to as SEQ ID NO: 338); CSTD YM[2MeTrp]KVCRTLD C (herein referred to as SEQ ID NO: 339); CSTD YM[4MeTrp]KVCRTLD C (herein referred to as SEQ ID NO: 340); CSTD YM[5MeTrp]KVCRTLD C (herein referred to as SEQ ID NO: 341); CSTD YM[6MeTrp]KVCRTLD C (herein referred to as SEQ ID NO: 342); CSTD YM[7MeTrp]KVCRTLD C (herein referred to as SEQ ID NO: 343); CSTD YM[AzaTrp]K VCRTLDC (herein referred to as SEQ ID NO: 344); CSTD YMW[HArg]VC RTLDC (herein referred to as SEQ ID NO: 345); CSTD YMW[Orn]VC RTLDC (herein referred to as SEQ ID NO: 346); CSTD YMW[Agb]VCRTLDC (herein referred to as SEQ ID NO: 347); CSTD YMWK[tBuGly]CRTLDC (herein referred to as SEQ ID NO: 348); CSTD YMWK[Cbg]CRTLDC (herein referred to as SEQ ID NO: 349); CSTD YMWK[C5g]CRTLDC (herein referred to as SEQ ID NO: 350); CSTD YMWK[3HyV]CRTLDC (herein referred to as SEQ ID NO: 351); CSTD YMWKVC[HArg]TLDC (herein referred to as SEQ ID NO: 352); CSTD YMWKVC[Arg(Me)]TLDC (herein referred to as SEQ ID NO: 353); CSTD YMWKVCR[3HyV]LD C (herein referred to as SEQ ID NO: 354); CSTD YMWKVCRT[tBuAla]DC (herein referred to as SEQ ID NO: 355); CSTD YMWKVCRT[Cba]D C (herein referred to as SEQ ID NO: 356); CSTD YMWKVCRT[Nva]DC (herein referred to as SEQ ID NO: 357); CSTD YMWKVCRT[Nle] DC (herein referred to as SEQ ID NO: 358); CTTDM AWR DCRTLDC (herein referred to as SEQ ID NO: 359); CTTDM AWR LCRTLDC (herein referred to as SEQ ID NO: 360); CTTDM VWK VCRTLDC (herein referred to as SEQ ID NO: 361); CVTD YMWKVCRTLDC (herein referred to as SEQ ID NO: 362); CYTD SMWKVCRTLDC (herein referred to as SEQ ID NO: 363); CTTDM MWKVCREP DC (herein referred to as SEQ ID NO: 364); CTTDM MWKVCRSM DC (herein referred to as SEQ ID NO: 365); and CTTDMMWKVCRTLDC (herein referred to as SEQ ID NO: 366). In some embodiments, the polypeptide comprising an amino acid sequence as described above, or a modified derivative thereof, or a salt thereof, is extended at the N-terminus. In some embodiments the polypeptide is extended at the N-terminus with one or more (e.g. from 1 to about 20, e.g. from 1 to about 10, or from 1 to about 5, e.g.1, 2, 3, 4 or 5) additional amino acids or analogues thereof. In some embodiments the polypeptide is extended at the C- terminus. In some embodiments the polypeptide is extended at the C-terminus with one or more (e.g. from 1 to about 20, e.g. from 1 to about 10, or from 1 to about 5, e.g.1, 2, 3, 4 or 5) additional amino acids or analogues thereof. In some embodiments the polypeptide is extended at the N-terminus and the C-terminus. In some embodiments the polypeptide is extended at the N-terminus and the C-terminus with one or more (e.g. from 1 to about 20, or from 1 to about 10, e.g. from 1 to about 5, e.g. 1, 2, 3, 4 or 5) additional amino acids or analogues thereof. In some embodiments the polypeptide is modified at the N- and / or C-terminus. In some embodiments the polypeptide is modified at the N- and C- terminus. Examples of N- terminal modifications include extension of the peptide by one or more amino acids or amino acid analogues such as alanine (A) or a variant thereof (such as dA), lysine (K) or a variant thereof, guanidinoacetic acid (GuanAc), pentynoic acid (PYA), N-terminal acetylation, UHSUHVHQWHG^E\^³$F´, or N-terminal carboximidamidation where the N-terminal amide of the peptide is modified with a -C(=N)NH2group so that it becomes a guanidine group, represented E\^³&,$´. In some embodiments, the polypeptide is modified at the N-terminus by extension by a sequence of 1 to 10 amino acids, for example 1 to 5 amino acids, or 3 to 5 amino acids. The amino acids may be natural amino acids. In some embodiments, the polypeptide is modified at the N-terminus by extension by an amino acid sequence selected from TVKTP, YYYEW, MRQ, EHM, EPKRQ, ANYAN, FSFHQ, AHGG, AIKP, ADST, ALNG, ALEQN, AHAGT, VNENI, and TNEGI. Examples of C-terminal modifications include extension of the peptide by one or more amino acids or amino acid analogs such as alanine (A) or a variant thereof (for example, CF3Ala, or dA), glutamic acid (E), serine (S), sarcosine (Sar), KFI, lysine (K) or a variant thereof. An example of a C-terminal modification is amidation; i.e. the conversion of a C- terminal carboxylic acid group (-C(O)OH or -C(O)O- to an amide -C(O)NH2). In some embodiments the C-terminus of the peptide is amidated. In some embodiments, the polypeptide is modified at the C-terminus by extension by a sequence of 1 to 10 amino acids, for example 1 to 8 amino acids, or 1 to 6 amino acids, or 3 to 6 amino acids. The amino acids may be natural amino acids. In some embodiments, the polypeptide is modified at the C- terminus by extension by an amino acid sequence selected from DKTTV, DIHNN, VYNVN, AGAAAE, KMTHE, NDSLN, SVNAN, QGHTPL, EMEHSN, ETP, TQS, EVHA, QHEA, QHPA, PLSA, NLNLK, RNPHD, and IHNNG. Examples of a variant of lysine are K(Ac), wherein Ac represents acetyl, and KFl where Fl represents fluorescein. Another example of a variant of lysine is K(PYA) or dK(PYA) wherein PYA represents pentynoic acid (e.g. 4-pentynoic acid). In some embodiments K(PYA) has the structure (e.g. prior to attachment to e.g. a linker such as an azide group comprised in a linker): In one embodiment, the polypeptide additionally comprises an N-terminal addition which is an alanine residue or Ac, and a C-terminal addition which is an alanine residue and / or K(PYA). In one embodiment, the polypeptide additionally comprises an N-terminal addition which is an alanine residue, and a C-terminal addition which is an alanine residue and / or K(PYA) (for example, a C-terminal addition -A-[K(PYA)]). In one embodiment, the polypeptide additionally comprises an N-terminal addition which is an alanine residue, and a C-terminal addition which is an alanine residue. Typically, the C-terminus is amidated. In one embodiment, the peptide ligand additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from A-(SEQ ID NO: 7)-A-[Sar6]-[KFl]; A-(SEQ ID NO: 7)-A; A-(SEQ ID NO: 8)-A; A-(SEQ ID NO: 8)-A-[K(PYA)]; A-(SEQ ID NO: 9)-A; A-(SEQ ID NO: 10)-A; A-(SEQ ID NO: 11)-A; A-(SEQ ID NO: 12)-A; A-(SEQ ID NO: 13)-A; A-(SEQ ID NO: 14)-A); A-(SEQ ID NO: 15)-A); A-(SEQ ID NO: 16)-A; A-(SEQ ID NO: 17)-A; A-(SEQ ID NO: 18)-A; A-(SEQ ID NO: 19)-A; A-(SEQ ID NO: 20)-A; A-(SEQ ID NO: 21)-A; A-(SEQ ID NO: 22)-A; A-(SEQ ID NO: 23)-A; A-(SEQ ID NO: 24)-A; A-(SEQ ID NO: 25)-A; A-(SEQ ID NO: 25)-A-[K(PYA)]; A-(SEQ ID NO: 25); Ac-A-(SEQ ID NO: 25); (SEQ ID NO: 25)-A; Ac-(SEQ ID NO: 25)-A; Ac-(SEQ ID NO: 25); Ac-A-(SEQ ID NO: 25)-A; A-(SEQ ID NO: 25)-DKTTV; TVKTP-(SEQ ID NO: 25)-A; A-(SEQ ID NO: 25)-DIHNN; A-(SEQ ID NO: 26)-A; A-(SEQ ID NO: 27)-A; A-(SEQ ID NO: 28)-A; A-(SEQ ID NO: 29)-A; A-(SEQ ID NO: 30)-A; A-(SEQ ID NO: 31)-A; A-(SEQ ID NO: 32)-A; A-(SEQ ID NO: 33)-A; A-(SEQ ID NO: 34)-A; A-(SEQ ID NO: 35)-A; A-(SEQ ID NO: 36)-A; A-(SEQ ID NO: 37)-A; A-(SEQ ID NO: 38)-A; A-(SEQ ID NO: 38)-A-[K(PYA)]; A-(SEQ ID NO: 38); (SEQ ID NO: 38)-A; Ac-(SEQ ID NO: 38); YYYE W-(SEQ ID NO: 38)-A; A-(SEQ ID NO: 39)-A; A-(SEQ ID NO: 40)-A; A-(SEQ ID NO: 41)-A; A-(SEQ ID NO: 42)-A; A-(SEQ ID NO: 43)-A; A-(SEQ ID NO: 44)-A; A-(SEQ ID NO: 45)-A; A-(SEQ ID NO: 46)-A; A-(SEQ ID NO: 47)-A; A-(SEQ ID NO: 48)-A; A-(SEQ ID NO: 49)-A; A-(SEQ ID NO: 50)-A; A-(SEQ ID NO: 51)-A; A-(SEQ ID NO: 52)-A; A-(SEQ ID NO: 53)-A; A-(SEQ ID NO: 54)-A; A-(SEQ ID NO: 55)-A; A-(SEQ ID NO: 56)-A; A-(SEQ ID NO: 57)-A; A-(SEQ ID NO: 58)-A; A-(SEQ ID NO: 59)-A; A-(SEQ ID NO: 59)-VYNVN; A-(SEQ ID NO: 60)-A; A-(SEQ ID NO: 61)-A; A-(SEQ ID NO: 62)-A; A-(SEQ ID NO: 63)-A; A-(SEQ ID NO: 63)-A-[K(PYA]; A-(SEQ ID NO: 64)-A; A-(SEQ ID NO: 65)-A; A-(SEQ ID NO: 65)-A-[Sar6] [KFl]; Ac-(SEQ ID NO: 66)-A-[K(PYA)]; Ac-(SEQ ID NO: 66)-[K(PYA)]; A-(SEQ ID NO: 66)-A-[K(PYA)]; A-(SEQ ID NO: 67)-A; A-(SEQ ID NO: 68)-A; A-(SEQ ID NO: 69)-A; A-(SEQ ID NO: 70)-A; A-(SEQ ID NO: 71)-A; A-(SEQ ID NO: 72)-A; A-(SEQ ID NO: 73)-A; A-(SEQ ID NO: 74)-A; A-(SEQ ID NO: 75)-A; A-(SEQ ID NO: 76)-A; A-(SEQ ID NO: 76)-A-[Sar6]-[KFl]; A-(SEQ ID NO: 76)-A-[K(PYA)]; A-(SEQ ID NO: 77)-A; A-(SEQ ID NO: 78)-A; A-(SEQ ID NO: 79)-A; A-(SEQ ID NO: 80)-A; A-(SEQ ID NO: 80)-A-[Sar6]-[KFl]; Ac-(SEQ ID NO: 80); A-(SEQ ID NO: 80)-A-[Sar6]-[K(Ac)]; A-(SEQ ID NO: 80)-AGAA AE; A-(SEQ ID NO: 81)-A; A-(SEQ ID NO: 82)-A); A-(SEQ ID NO: 83)-A; A-(SEQ ID NO: 84)-A; A-(SEQ ID NO: 85)-A; A-(SEQ ID NO: 86)-A; A-(SEQ ID NO: 87)-A; A-(SEQ ID NO: 88)-A; Ac-(SEQ ID NO: 89); A-(SEQ ID NO: 90)-A); A-(SEQ ID NO: 91)-A; A-(SEQ ID NO: 91)-A-[Sar6]-[KFl]; A-(SEQ ID NO: 92)-A; A-(SEQ ID NO: 93)-A; A-(SEQ ID NO: 94)-A; A-(SEQ ID NO: 95)-A; A-(SEQ ID NO: 95)-A-[Sar6]-[KFl]; A-(SEQ ID NO: 95)-A-[K(PYA)]; Ac-(SEQ ID NO: 95); A-(SEQ ID NO: 96)-A; Ac-(SEQ ID NO: 96); Ac-(SEQ ID NO: 97); Ac-(SEQ ID NO: 98); Ac-(SEQ ID NO: 99); Ac-(SEQ ID NO: 100); Ac-(SEQ ID NO: 101); Ac-(SEQ ID NO: 102); Ac-(SEQ ID NO: 103); Ac-(SEQ ID NO: 104); A-(SEQ ID NO: 105)-A; A-(SEQ ID NO: 105)-A-[K(PYA)]; A-(SEQ ID NO: 106)-A-[K(PYA)]; A-(SEQ ID NO: 107)-A; A-(SEQ ID NO: 107)-A-[Sar6]-[KFl]; A-(SEQ ID NO: 108)-A; A-(SEQ ID NO: 108)-A-[K(PYA)]; Ac-(SEQ ID NO: 108)-[K(PYA)]; Ac-A-(SEQ ID NO: 108)-A-[K(PYA)]; A-(SEQ ID NO: 108)-A-[Sar6]-[(K(Ac)]; A-(SEQ ID NO: 108)-AGAA AE; A-(SEQ ID NO: 108)-KMTH E; A-(SEQ ID NO: 108)-NDSLN; A-(SEQ ID NO: 108)-SVNAN ; A-(SEQ ID NO: 108)-QGH TPL; A-(SEQ ID NO: 108)-EMEH SN; MR Q-(SEQ ID NO: 108)-ETP; EHM-(SEQ ID NO: 108)-TQ S; EPKR Q-(SEQ ID NO: 108)-A; ANYA N-(SEQ ID NO: 108)-A; DSFH Q-(SEQ ID NO: 108)-A; MRQ-(SEQ ID NO: 108)-ETP-[K(PYA)]; EPKR Q-(SEQ ID NO: 108)-A-[K(PYA)]; Ac-(SEQ ID NO: 108)-A-[K(PYA)]; Ac-(SEQ ID NO: 108)-E-[K(PYA)]; A-(SEQ ID NO: 108)-E-[K(PYA)]; A-(SEQ ID NO: 109)-A-[K(PYA)]; A-(SEQ ID NO: 110)-A-[K(PYA)]; A-(SEQ ID NO: 111)-A-[K(PYA)]; A-(SEQ ID NO: 112)-A-[K(PYA)]; A-(SEQ ID NO: 113)-A-[K(PYA)]; A-(SEQ ID NO: 114)-A-[K(PYA)]; A-(SEQ ID NO: 115)-A-[K(PYA)]; A-(SEQ ID NO: 116)-A-[K(PYA)]; A-(SEQ ID NO: 117)-A; A-(SEQ ID NO: 117)-A-[K(PYA)]; Ac-(SEQ ID NO: 117)-[K(PYA)]; A-(SEQ ID NO: 118)-A-[K(PYA)]; A-(SEQ ID NO: 119)-A-[K(PYA)]; MRQ-(SEQ ID NO: 119)-ETP-[K(PYA)]; EPKR Q-(SEQ ID NO: 119)-A-[K(PYA)]; MRQ-(SEQ ID NO: 119)-ETP; EPKR Q-(SEQ ID NO: 119)-A; Ac-(SEQ ID NO: 119)-[K(PYA)]; A-(SEQ ID NO: 120)-A-[K(PYA)]; A-(SEQ ID NO: 121)-A-[K(PYA)]; A-(SEQ ID NO: 122)-A-[K(PYA)]; A-(SEQ ID NO: 123)-A-[K(PYA)]; A-(SEQ ID NO: 124)-A-[K(PYA)]; A-(SEQ ID NO: 125)-A-[K(PYA)]; A-(SEQ ID NO: 126)-A-[K(PYA)]; [dA]-(SEQ ID NO: 127)-[dA]-[K(PYA)]; A-(SEQ ID NO: 128)-A-[K(PYA)]; A-(SEQ ID NO: 129)-A; A-(SEQ ID NO: 129); Ac-(SEQ ID NO: 129); A-(SEQ ID NO: 130); Ac-(SEQ ID NO: 130); Ac-(SEQ ID NO: 131)-[K(PYA)]; Ac-(SEQ ID NO: 132)-[K(PYA)]; Ac-(SEQ ID NO: 132)-[K(PYA)-(Triazolyl)-(PEG)2-methyl]; Ac-(SEQ ID NO: 133)-[K(PYA)]; Ac-(SEQ ID NO: 134)-[K(PYA)]; Ac-(SEQ ID NO: 135)-[K(PYA)]; Ac-(SEQ ID NO: 136)-[K(PYA)]; Ac-(SEQ ID NO: 136)-[K(PYA)-(Triazolyl)-(PEG)2-methyl]; A-(SEQ ID NO: 137)-A; A-(SEQ ID NO: 138)-A; A-(SEQ ID NO: 138)-A-[Sar6] -[KFl]; A-(SEQ ID NO: 138)-A-[K(PYA)]; A-(SEQ ID NO: 139)-A; A-(SEQ ID NO: 139)-A-[Sar6] -[KFl]; A-(SEQ ID NO: 140)-A; A-(SEQ ID NO: 141)-A; A-(SEQ ID NO: 141)-A-[Sar6] -[KFl]; A-(SEQ ID NO: 142)-A; A-(SEQ ID NO: 143)-A; A-(SEQ ID NO: 143)-A-[K(PYA)]; A-(SEQ ID NO: 144)-A; A-(SEQ ID NO: 144)-A-[K(PYA)]; Ac-A-(SEQ ID NO: 144)-A; Ac-(SEQ ID NO: 144); A-(SEQ ID NO: 144); Ac-A-(SEQ ID NO: 144); (SEQ ID NO: 144)-A; Ac-(SEQ ID NO: 144)-A; AHG G-(SEQ ID NO: 144)-EVHA; AI KP-(SEQ ID NO: 144)-QHEA; ADST-(SEQ ID NO: 144)-QH PA; ALNG-(SEQ ID NO: 144)-PLS A; ALNG-(SEQ ID NO: 144)-PLS A-[K(PYA)]; A-(SEQ ID NO: 145)-A; A-(SEQ ID NO: 146)-A; A-(SEQ ID NO: 147)-A; A-(SEQ ID NO: 148)-A; A-(SEQ ID NO: 149)-A; A-(SEQ ID NO: 150)-A; A-(SEQ ID NO: 151)-A; A-(SEQ ID NO: 152)-A; A-(SEQ ID NO: 153)-A; A-(SEQ ID NO: 154)-A; A-(SEQ ID NO: 155)-A; A-(SEQ ID NO: 156)-A; A-(SEQ ID NO: 157)-A; A-(SEQ ID NO: 158)-A; A-(SEQ ID NO: 159)-A; A-(SEQ ID NO: 160)-A; A-(SEQ ID NO: 161)-A; A-(SEQ ID NO: 162)-A; A-(SEQ ID NO: 163)-A; A-(SEQ ID NO: 164)-A; A-(SEQ ID NO: 165)-A; A-(SEQ ID NO: 166)-A; A-(SEQ ID NO: 167)-A; A-(SEQ ID NO: 168)-A; A-(SEQ ID NO: 169)-A; A-(SEQ ID NO: 170)-A; A-(SEQ ID NO: 171)-A; A-(SEQ ID NO: 172)-A; A-(SEQ ID NO: 173)-A; A-(SEQ ID NO: 174)-A; A-(SEQ ID NO: 175)-A; A-(SEQ ID NO: 176)-A; A-(SEQ ID NO: 177)-A; A-(SEQ ID NO: 178)-A; A-(SEQ ID NO: 179)-A; A-(SEQ ID NO: 180)-A; A-(SEQ ID NO: 181)-A; A-(SEQ ID NO: 182)-A; A-(SEQ ID NO: 183)-A; A-(SEQ ID NO: 184)-A; A-(SEQ ID NO: 185)-A; A-(SEQ ID NO: 186)-A; A-(SEQ ID NO: 187)-A; A-(SEQ ID NO: 188)-A; A-(SEQ ID NO: 189)-A; A-(SEQ ID NO: 190)-A; A-(SEQ ID NO: 191)-A; ALNG-(SEQ ID NO: 192)-PLS A; ALNG-(SEQ ID NO: 192)-PLS A-[K(PYA)]; ALNG-(SEQ ID NO: 193)-PLS A; ALNG-(SEQ ID NO: 193)-PLS A-[K(PYA)]; ALEQ N-(SEQ ID NO: 194)-A; ALEQ N-(SEQ ID NO: 194)-A-[K(PYA)]; ALEQ N-(SEQ ID NO: 195)-A; ALEQ N-(SEQ ID NO: 195)-A-[K(PYA)]; and AHAG T-(SEQ ID NO: 196)-A; A-(SEQ ID NO: 197)-A; A-(SEQ ID NO: 197)-A-[K(PYA)]; A-(SEQ ID NO: 197)-A-[Sar6]-[K(Ac)]; A-(SEQ ID NO: 198)-A; Ac-A-(SEQ ID NO: 198)-A; A-(SEQ ID NO: 198)-NLNLK; VNEN I-(SEQ ID NO: 198)-A; A-(SEQ ID NO: 198)-RNPH D; A-(SEQ ID NO: 198)-IHN NG; TNEG I-(SEQ ID NO: 198)-A; VNEN I-(SEQ ID NO: 198)-A-[K(PYA)]; A-(SEQ ID NO: 199)-A; A-(SEQ ID NO: 200)-A; A-(SEQ ID NO: 201)-A; A-(SEQ ID NO: 202)-A; A-(SEQ ID NO: 203)-A; A-(SEQ ID NO: 204)-A; A-(SEQ ID NO: 205)-A; A-(SEQ ID NO: 206)-A; A-(SEQ ID NO: 207)-A; A-(SEQ ID NO: 208)-A; A-(SEQ ID NO: 209)-A; A-(SEQ ID NO: 210)-A; A-(SEQ ID NO: 211)-A; A-(SEQ ID NO: 212)-A; A-(SEQ ID NO: 213)-A; A-(SEQ ID NO: 214)-A; A-(SEQ ID NO: 215)-A; A-(SEQ ID NO: 216)-A; A-(SEQ ID NO: 217)-A; A-(SEQ ID NO: 218)-A; A-(SEQ ID NO: 219)-A; A-(SEQ ID NO: 220)-A; A-(SEQ ID NO: 221)-A; A-(SEQ ID NO: 222)-A; A-(SEQ ID NO: 223)-A; A-(SEQ ID NO: 224)-A; A-(SEQ ID NO: 225)-A; A-(SEQ ID NO: 226)-A; and A-(SEQ ID NO: 226)-A-[K(PYA)]; A-(SEQ ID NO: 227)-A; A-(SEQ ID NO: 228)-A; A-(SEQ ID NO: 229)-A; and A-(SEQ ID NO: 229)-A-[K(PYA)]; A-(SEQ ID NO: 230)-A; A-(SEQ ID NO: 230)-A-[Sar6]-[KFl]; A-(SEQ ID NO: 231)-A; A-(SEQ ID NO: 232)-A; A-(SEQ ID NO: 232)-A-[Sar6]-[KFl]; A-(SEQ ID NO: 232)-A-[Sar6]-[K(Ac)]; A-(SEQ ID NO: 232)-AGAA AE; A-(SEQ ID NO: 233)-A; A-(SEQ ID NO: 234)-A; A-(SEQ ID NO: 235)-A; A-(SEQ ID NO: 236)-A; A-(SEQ ID NO: 237)-A; A-(SEQ ID NO: 238)-A; A-(SEQ ID NO: 239)-A; A-(SEQ ID NO: 240)-A; A-(SEQ ID NO: 241)-A; A-(SEQ ID NO: 242)-A; A-(SEQ ID NO: 243)-A; A-(SEQ ID NO: 244)-A; A-(SEQ ID NO: 245)-A; A-(SEQ ID NO: 246)-A; A-(SEQ ID NO: 247)-A); A-(SEQ ID NO: 248)-A; A-(SEQ ID NO: 249)-A; A-(SEQ ID NO: 249)-A-[Sar6]-[KFl]; Ac-A-(SEQ ID NO: 249)-A; A-(SEQ ID NO: 250)-A; A-(SEQ ID NO: 251)-A; A-(SEQ ID NO: 251)-A-[K(PYA)]; A-(SEQ ID NO: 252)-A; A-(SEQ ID NO: 253)-A; A-(SEQ ID NO: 254)-A; A-(SEQ ID NO: 255)-A; A-(SEQ ID NO: 256)-A; A-(SEQ ID NO: 257)-A; A-(SEQ ID NO: 258)-A; A-(SEQ ID NO: 258)-A-[Sar6]-[KFl]; A-(SEQ ID NO: 258)-A-[K(PYA)]; Ac-A-(SEQ ID NO: 258)-A; A-(SEQ ID NO: 259)-A; A-(SEQ ID NO: 260)-A; A-(SEQ ID NO: 260)-A-[K(PYA)]; A-(SEQ ID NO: 261)-A; A-(SEQ ID NO: 261)-A-[K(PYA)]; [PYA]-A-(SEQ ID NO: 261)-A; Ac-(SEQ ID NO: 261); A-(SEQ ID NO: 261); Ac-A-(SEQ ID NO: 261); [PYA]-(SEQ ID NO: 261); [GuanAc]-(SEQ ID NO: 261)-A; A-(SEQ ID NO: 261)-[CF3Ala]; A-(SEQ ID NO: 261)-S; A-(SEQ ID NO: 262)-A; A-(SEQ ID NO: 263)-A; A-(SEQ ID NO: 264)-A; A-(SEQ ID NO: 265)-A; A-(SEQ ID NO: 266)-A; A-(SEQ ID NO: 266); A-(SEQ ID NO: 267)-A; A-(SEQ ID NO: 267)-A-[K(PYA)]; Ac-(SEQ ID NO: 268); A-(SEQ ID NO: 268); [PYA]-(SEQ ID NO: 268); A-(SEQ ID NO: 269); Ac-(SEQ ID NO: 270); Ac-(SEQ ID NO: 271); A-(SEQ ID NO: 272)-A; A-(SEQ ID NO: 273)-A; A-(SEQ ID NO: 274)-A; A-(SEQ ID NO: 275)-A; A-(SEQ ID NO: 276)-A; A-(SEQ ID NO: 277)-A; A-(SEQ ID NO: 278)-A; A-(SEQ ID NO: 279)-A; A-(SEQ ID NO: 280)-A; A-(SEQ ID NO: 281)-A; A-(SEQ ID NO: 282)-A; A-(SEQ ID NO: 283)-A; A-(SEQ ID NO: 284)-A; A-(SEQ ID NO: 285)-A; A-(SEQ ID NO: 286)-A; A-(SEQ ID NO: 287)-A; A-(SEQ ID NO: 288)-A; A-(SEQ ID NO: 289)-A; A-(SEQ ID NO: 290)-A; A-(SEQ ID NO: 291)-A; A-(SEQ ID NO: 292)-A; A-(SEQ ID NO: 293)-A; A-(SEQ ID NO: 294)-A; [GuanAc]-(SEQ ID NO: 295)-COOH; [GuanAc]-(SEQ ID NO: 295); [CIA]-[K(PYA)]-(SEQ ID NO: 295)-A; [CIA]-[dK(PYA)]-(SEQ ID NO: 295)-A; [GuanAc]-(SEQ ID NO: 296); [GuanAc]-(SEQ ID NO: 297); [GuanAc]-(SEQ ID NO: 298); [GuanAc]-(SEQ ID NO: 299); [GuanAc]-(SEQ ID NO: 300); [GuanAc]-(SEQ ID NO: 301); [GuanAc]-(SEQ ID NO: 302); A-(SEQ ID NO: 303)-A; A-(SEQ ID NO: 304)-A; A-(SEQ ID NO: 305)-A-[K(PYA)]; A-(SEQ ID NO: 306)-A; A-(SEQ ID NO: 307)-A; A-(SEQ ID NO: 308)-A; A-(SEQ ID NO: 309)-A; A-(SEQ ID NO: 309)-A-[K(PYA)]; Ac-(SEQ ID NO: 309); Ac-A-(SEQ ID NO: 309)-A; [dA]-(SEQ ID NO: 309)-A; A-(SEQ ID NO: 309); Ac-A-(SEQ ID NO: 309); (SEQ ID NO: 309)-A; Ac-(SEQ ID NO: 309)-A; A-(SEQ ID NO: 309)-A-[dK(PYA)]; A-(SEQ ID NO: 309)-[K(PYA)]; A-(SEQ ID NO: 309)-[dK(PYA)]; A-(SEQ ID NO: 310)-A; A-(SEQ ID NO: 310)-A-[K(PYA)]; A-(SEQ ID NO: 311)-A; A-(SEQ ID NO: 312)-A; A-(SEQ ID NO: 313)-A; A-(SEQ ID NO: 314)-A; A-(SEQ ID NO: 315)-A; A-(SEQ ID NO: 316)-A; A-(SEQ ID NO: 317)-A; A-(SEQ ID NO: 318)-A; A-(SEQ ID NO: 319)-A; A-(SEQ ID NO: 320)-A; A-(SEQ ID NO: 321)-A; A-(SEQ ID NO: 322)-A; A-(SEQ ID NO: 323)-A; A-(SEQ ID NO: 324)-A; A-(SEQ ID NO: 325)-A; A-(SEQ ID NO: 326)-A; A-(SEQ ID NO: 327)-A; A-(SEQ ID NO: 328)-A; A-(SEQ ID NO: 329)-A; A-(SEQ ID NO: 330)-A; A-(SEQ ID NO: 331)-A; A-(SEQ ID NO: 332)-A; A-(SEQ ID NO: 333)-A; A-(SEQ ID NO: 334)-A; A-(SEQ ID NO: 335)-A; A-(SEQ ID NO: 336)-A; A-(SEQ ID NO: 337)-A; A-(SEQ ID NO: 338)-A; A-(SEQ ID NO: 339)-A; A-(SEQ ID NO: 340)-A; A-(SEQ ID NO: 341)-A; A-(SEQ ID NO: 342)-A; A-(SEQ ID NO: 343)-A; A-(SEQ ID NO: 344)-A; A-(SEQ ID NO: 345)-A; A-(SEQ ID NO: 346)-A; A-(SEQ ID NO: 347)-A; A-(SEQ ID NO: 348)-A; A-(SEQ ID NO: 349)-A; A-(SEQ ID NO: 350)-A; A-(SEQ ID NO: 351)-A; A-(SEQ ID NO: 352)-A; A-(SEQ ID NO: 353)-A; A-(SEQ ID NO: 354)-A; A-(SEQ ID NO: 355)-A; A-(SEQ ID NO: 356)-A; A-(SEQ ID NO: 357)-A; A-(SEQ ID NO: 358)-A; A-(SEQ ID NO: 359)-A; A-(SEQ ID NO: 360)-A; A-(SEQ ID NO: 361)-A; A-(SEQ ID NO: 362)-A; A-(SEQ ID NO: 363)-A; A-(SEQ ID NO: 364)-A; A-(SEQ ID NO: 365)-A; and A-(SEQ ID NO: 366)-A. In some embodiments a peptide ligand as provided herein comprises a peptide as provided herein attached to a molecular scaffold. The molecular scaffold can be any molecular scaffold as described in more detail herein. In some embodiments the molecular scaffold is attached to one or more reactive groups in the peptide. In some embodiments the molecular scaffold is attached to one or more reactive groups e.g. to one or more cysteine or cysteamine groups (e.g. to the thiol group comprised in the cysteine or cysteamine side chain) in the peptide. In some embodiments the peptide comprises three cysteine residues (L-cysteine and / or D- cysteine) and the molecular scaffold is attached to the three cysteine groups. One example of a molecule suitable for use as a molecular scaffold in the peptide ligands and complexes comprising them as provided herein is TATA (1,3,5-Triacryloylhexahydro-1,3,5- triazine, available from Sigma Aldrich). TATA has the structure: In some embodiments TATA reacts with cysteinyl-thiol groups of peptides as described herein to form a peptide ligand comprising a scaffold which is a derivative of TATA of form: wherein each Cys-S represents a cysteine residue (e.g. L-cysteine or D-cysteine) or cysteamine residue. Accordingly, in one embodiment, the molecular scaffold is a derivative of TATA which has the following structure: , which can also be depicted as wherein * denotes the point of attachment of the three (e.g.) cysteine residues. In an alternative embodiment, the molecular scaffold is 1,3,5-tris(bromoacetyl) hexahydro-1, 3,5-triazine (TATB): TATB. Thus, following cyclisation with the bicyclic peptides of the invention on (e.g.) the cysteine residues, the molecular scaffold forms a tri-substituted 1,3,5-tris(bromoacetyl) hexahydro-1,3, 5-triazine derivative of TATB having the following structure: which may also be depicted as wherein * denotes the point of attachment of the three cysteine residues. In an alternative embodiment, the molecular scaffold is 2,4,6-tris(bromomethyl)-s-triazine (TBMT): Thus, following cyclisation with the bicyclic peptides of the invention on the Ci, Cii, and Ciiicysteine residues, the molecular scaffold forms a tri-substituted 2,4,6-tris(bromomethyl)-s- triazine derivative of TBMT having the following structure: which may also be depicted as wherein * denotes the point of attachment of the (e.g.) three cysteine residues. In an alternative embodiment, the molecular scaffold is 2,4,6-tris(chloromethyl)-1,3,5-triazine (TCTZ): TCTZ. Thus, following cyclisation with the bicyclic peptides of the invention on the Ci, Cii, and Ciiicysteine residues, the molecular scaffold forms a tri-substituted 2,4,6-tris(chloromethyl)-s- triazine derivative of TCTZ having the following structure: wherein * denotes the point of attachment of the (e.g.) three cysteine residues. It will be appreciated that, following cyclisation of the bicyclic peptides of the invention with either TBMT or TCTZ, the derivatives of TBMT and TCTZ which form the molecular scaffold have the same structure, as represented above. Therefore, where reference is made herein to a molecular scaffold which is a derivative of TBMT, the molecular scaffold may also be a derivative of TCTZ. Thus, according to a further aspect of the invention, there is provided a bicyclic peptide ligand capable of binding TLR3, or a pharmaceutically acceptable salt thereof, which comprises a peptide ligand comprising a polypeptide comprising three reactive groups, wherein the polypeptide is attached to a molecular scaffold. According to a further aspect of the invention, there is provided a bicyclic peptide ligand capable of binding TLR3 which comprises a peptide ligand as described herein, and a molecular scaffold, wherein the three cysteine (L-cysteine or D-cysteine) or Cysam residues of said peptide ligand form covalent bonds with the molecular scaffold to form two loop sequences. In one embodiment, provided herein is a bicycle peptide ligand comprising a peptide of SEQ ID NO: 1, or a modified derivative thereof, optionally extended at the N- and / or C- terminus, or a pharmaceutically acceptable salt thereof, bonded at each of three reactive residues (e.g. at each of the three cysteine residues (e.g. L-cysteine or D-cysteine)) to a molecular scaffold which is a derivative of TATA, TATB, TBMT or TCTZ as described herein. In one embodiment said bicycle ligand comprises a peptide sequence of SEQ ID NO: 7 to 61. In one embodiment said bicycle ligand comprises a peptide sequence of SEQ ID NO: 7 to 23, and the molecular scaffold is a derivative of TATA as described herein. In one embodiment said bicycle ligand comprises a peptide sequence of SEQ ID NO: 24 to 37, and the molecular scaffold is a derivative of TATB as described herein. In one embodiment said bicycle ligand comprises a peptide sequence of SEQ ID NO: 38 to 61, and the molecular scaffold is a derivative of TBMT or TCTZ as described herein. In one embodiment, provided herein is a bicycle peptide ligand comprising a peptide of SEQ ID NO: 2, or a modified derivative thereof, optionally extended at the N- and / or C- terminus, or a pharmaceutically acceptable salt thereof, bonded at each of three reactive residues (e.g. at each of the three cysteine residues (e.g. L-cysteine or D-cysteine)) to a molecular scaffold which is a derivative of TBMT or TCTZ as described herein. In one embodiment said bicycle ligand comprises a peptide sequence of SEQ ID NO: 62 to 64. In one embodiment, provided herein is a bicycle peptide ligand comprising a peptide of SEQ ID NO: 3, or a modified derivative thereof, optionally extended at the N- and / or C- terminus, or a pharmaceutically acceptable salt thereof, bonded at each of three reactive residues (e.g. at each of the three cysteine / cysteamine residues (e.g. L-cysteine or D- cysteine)) to a molecular scaffold which is a derivative of TATA or TATB as described herein. In one embodiment said bicycle ligand comprises a peptide sequence of SEQ ID NO: 65 to 196. In one embodiment said bicycle ligand comprises a peptide sequence of SEQ ID NO: 65 to 141, and the molecular scaffold is a derivative of TATA as described herein. In one embodiment said bicycle ligand comprises a peptide sequence of SEQ ID NO: 142 to 196, and the molecular scaffold is a derivative of TATB as described herein. In one embodiment, provided herein is a bicycle peptide ligand comprising a peptide of SEQ ID NO: 4, or a modified derivative thereof, optionally extended at the N- and / or C- terminus, or a pharmaceutically acceptable salt thereof, bonded at each of three reactive residues (e.g. at each of the three cysteine residues (e.g. L-cysteine or D-cysteine)) to a molecular scaffold which is a derivative of TATB as described herein. In one embodiment said bicycle ligand comprises a peptide sequence of SEQ ID NO: 197 to 226. In one embodiment, provided herein is a bicycle peptide ligand comprising a peptide of SEQ ID NO: 5, or a modified derivative thereof, optionally extended at the N- and / or C- terminus, or a pharmaceutically acceptable salt thereof, bonded at each of three reactive residues (e.g. at each of the three cysteine residues (e.g. L-cysteine or D-cysteine)) to a molecular scaffold which is a derivative of TBMT or TCTZ as described herein. In one embodiment said bicycle ligand comprises a peptide sequence of SEQ ID NO: 227 to 229. In one embodiment, provided herein is a bicycle peptide ligand comprising a peptide of SEQ ID NO: 6, or a modified derivative thereof, optionally extended at the N- and / or C- terminus, or a pharmaceutically acceptable salt thereof, bonded at each of three reactive residues (e.g. at each of the three cysteine / cysteamine residues (e.g. L-cysteine or D- cysteine)) to a molecular scaffold which is a derivative of TATA , TBMT or TCTZ as described herein. In one embodiment said bicycle ligand comprises a peptide sequence of SEQ ID NO: 230 to 366. In one embodiment said bicycle ligand comprises a peptide sequence of SEQ ID NO: 230 to 259, and the molecular scaffold is a derivative of TATA as described herein. In one embodiment said bicycle ligand comprises a peptide sequence of SEQ ID NO: 260 to 366, and the molecular scaffold is a derivative of TBMT or TCTZ as described herein. In a further embodiment, the molecular scaffold is a derivative of TATA which has the following structure: wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of C-X1-X2-X3-C-X4-X5-X6-X7-X8-X9-C (SEQ ID NO: 1) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 7)-A-[Sar6]-[KFl] (herein referred to as BCY15200); A-(SEQ ID NO: 7)-A (herein referred to as BCY15212); A-(SEQ ID NO: 8)-A (herein referred to as BCY15747); A-(SEQ ID NO: 8)-A-[K(PYA)] (herein referred to as BCY19281); A-(SEQ ID NO: 9)-A (herein referred to as BCY17064); A-(SEQ ID NO: 10)-A (herein referred to as BCY17065); A-(SEQ ID NO: 11)-A (herein referred to as BCY17066); A-(SEQ ID NO: 12)-A (herein referred to as BCY17067); A-(SEQ ID NO: 13)-A (herein referred to as BCY17068); A-(SEQ ID NO: 14)-A (herein referred to as BCY17070); A-(SEQ ID NO: 15)-A (herein referred to as BCY17071); A-(SEQ ID NO: 16)-A (herein referred to as BCY17072); A-(SEQ ID NO: 17)-A (herein referred to as BCY17079); A-(SEQ ID NO: 18)-A (herein referred to as BCY17080); A-(SEQ ID NO: 19)-A (herein referred to as BCY17081); A-(SEQ ID NO: 20)-A (herein referred to as BCY16675); A-(SEQ ID NO: 21)-A (herein referred to as BCY16676); A-(SEQ ID NO: 22)-A (herein referred to as BCY16677); and A-(SEQ ID NO: 23)-A (herein referred to as BCY16678); or a modified derivative and / or pharmaceutically acceptable salt thereof. In a further embodiment, the molecular scaffold is a derivative of TATB which has the following structure: wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of C-X1-X2-X3-C-X4-X5-X6-X7-X8-X9-C (SEQ ID NO: 1) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 24)-A (herein referred to as BCY16997); A-(SEQ ID NO: 25)-A (herein referred to as BCY18125); A-(SEQ ID NO: 25)-A-[K(PYA)] (herein referred to as BCY19741); A-(SEQ ID NO: 25) (herein referred to as BCY21538); Ac-A-(SEQ ID NO: 25) (herein referred to as BCY21539); (SEQ ID NO: 25)-A (herein referred to as BCY21540); Ac-(SEQ ID NO: 25)-A (herein referred to as BCY21541); Ac-(SEQ ID NO: 25) (herein referred to as BCY21543); Ac-A-(SEQ ID NO: 25)-A (herein referred to as BCY21544); A-(SEQ ID NO: 25)-DKTTV (herein referred to as BCY21769); TVKTP-(SEQ ID NO: 25)-A (herein referred to as BCY21775); A-(SEQ ID NO: 25)-DIHNN (herein referred to as BCY21777); A-(SEQ ID NO: 26)-A (herein referred to as BCY21550); A-(SEQ ID NO: 27)-A (herein referred to as BCY21551); A-(SEQ ID NO: 28)-A (herein referred to as BCY21558); A-(SEQ ID NO: 29)-A (herein referred to as BCY21561); A-(SEQ ID NO: 30)-A (herein referred to as BCY21562); A-(SEQ ID NO: 31)-A (herein referred to as BCY21564); A-(SEQ ID NO: 32)-A (herein referred to as BCY21565); A-(SEQ ID NO: 33)-A (herein referred to as BCY21566); A-(SEQ ID NO: 34)-A (herein referred to as BCY21567); A-(SEQ ID NO: 35)-A (herein referred to as BCY21568); A-(SEQ ID NO: 36)-A (herein referred to as BCY21569); and A-(SEQ ID NO: 37)-A (herein referred to as BCY16998); or a modified derivative and / or pharmaceutically acceptable salt thereof. In a further embodiment, the molecular scaffold is a tri-substituted 2,4,6-tris(bromomethyl)-s- triazine derivative of TBMT or TCTZ having the following structure: wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of C-X1-X2-X3-C-X4-X5-X6-X7-X8-X9-C (SEQ ID NO: 1) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 38)-A (herein referred to as BCY18251); A-(SEQ ID NO: 38)-A-[K(PYA)] (herein referred to as BCY19587); A-(SEQ ID NO: 38) (herein referred to as BCY21493); (SEQ ID NO: 38)-A (herein referred to as BCY21495); Ac-(SEQ ID NO: 38) (herein referred to as BCY21498); YYYE W-(SEQ ID NO: 38)-A (herein referred to as BCY21773); A-(SEQ ID NO: 39)-A (herein referred to as BCY21485); A-(SEQ ID NO: 40)-A (herein referred to as BCY21490); A-(SEQ ID NO: 41)-A (herein referred to as BCY21500); A-(SEQ ID NO: 42)-A (herein referred to as BCY21502); A-(SEQ ID NO: 43)-A (herein referred to as BCY21503); A-(SEQ ID NO: 44)-A (herein referred to as BCY21504); A-(SEQ ID NO: 45)-A (herein referred to as BCY21505); A-(SEQ ID NO: 46)-A (herein referred to as BCY21506); A-(SEQ ID NO: 47)-A (herein referred to as BCY21507); A-(SEQ ID NO: 48)-A (herein referred to as BCY21508); A-(SEQ ID NO: 49)-A (herein referred to as BCY21510); A-(SEQ ID NO: 50)-A (herein referred to as BCY21515); A-(SEQ ID NO: 51)-A (herein referred to as BCY21517); A-(SEQ ID NO: 52)-A (herein referred to as BCY21518); A-(SEQ ID NO: 53)-A (herein referred to as BCY21519); A-(SEQ ID NO: 54)-A (herein referred to as BCY21521); A-(SEQ ID NO: 55)-A (herein referred to as BCY21522); A-(SEQ ID NO: 56)-A (herein referred to as BCY21523); A-(SEQ ID NO: 57)-A (herein referred to as BCY21527); A-(SEQ ID NO: 58)-A (herein referred to as BCY21528); A-(SEQ ID NO: 59)-A (herein referred to as BCY19930); A-(SEQ ID NO: 59)-VYNVN (herein referred to as BCY21776 ); A-(SEQ ID NO: 60)-A (herein referred to as BCY19931); and A-(SEQ ID NO: 61)-A (herein referred to as BCY19932); or a modified derivative and / or pharmaceutically acceptable salt thereof. In a further embodiment, the molecular scaffold is a tri-substituted 2,4,6-tris(bromomethyl)-s- triazine derivative of TBMT or TCTZ having the following structure: wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of C-X10-X11-Y-Y-C-X12-Q-T-X13-X14-F-C (SEQ ID NO: 2) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 62)-A (herein referred to as BCY17006); A-(SEQ ID NO: 63)-A (herein referred to as BCY18134); A-(SEQ ID NO: 63)-A-[K(PYA] (herein referred to as BCY19746); and A-(SEQ ID NO: 64)-A (herein referred to as BCY17012); or a modified derivative and / or pharmaceutically acceptable salt thereof. In a further embodiment, the molecular scaffold is a derivative of TATA which has the following structure: wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of X15-X16-X17-X18-X19-X20-X21-X22-X23-X24-X25-X26-X27-X28-X29(SEQ ID NO: 3) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 65)-A (herein referred to as BCY15206); A-(SEQ ID NO: 65)-A-[Sar6] [KFl] (herein referred to as BCY15194); Ac-(SEQ ID NO: 66)-A-[K(PYA)] (herein referred to as BCY23135); Ac-(SEQ ID NO: 66)-[K(PYA)] (herein referred to as BCY23136); A-(SEQ ID NO: 66)-A-[K(PYA)] (herein referred to as BCY20791); A-(SEQ ID NO: 67)-A (herein referred to as BCY15808); A-(SEQ ID NO: 68)-A (herein referred to as BCY15810); A-(SEQ ID NO: 69)-A (herein referred to as BCY16655); A-(SEQ ID NO: 70)-A (herein referred to as BCY16656); A-(SEQ ID NO: 71)-A (herein referred to as BCY16657); A-(SEQ ID NO: 72)-A (herein referred to as BCY16658); A-(SEQ ID NO: 73)-A (herein referred to as BCY16659); A-(SEQ ID NO: 74)-A (herein referred to as BCY16660); A-(SEQ ID NO: 75)-A (herein referred to as BCY16661); A-(SEQ ID NO: 76)-A (herein referred to as BCY15207); A-(SEQ ID NO: 76)-A-[Sar6]-[KFl] (herein referred to as BCY15195); A-(SEQ ID NO: 76)-A-[K(PYA)] (herein referred to as BCY15750); A-(SEQ ID NO: 77)-A (herein referred to as BCY15811); A-(SEQ ID NO: 78)-A (herein referred to as BCY15812); A-(SEQ ID NO: 79)-A (herein referred to as BCY15813); A-(SEQ ID NO: 80)-A (herein referred to as BCY15814); A-(SEQ ID NO: 80)-A-[Sar6]-[KFl] (herein referred to as BCY15801); Ac-(SEQ ID NO: 80) (herein referred to as BCY17031); A-(SEQ ID NO: 80)-A-[Sar6]-[K(Ac)] (herein referred to as BCY19384); A-(SEQ ID NO: 80)-AGAA AE (herein referred to as BCY19582); A-(SEQ ID NO: 81)-A (herein referred to as BCY17032); A-(SEQ ID NO: 82)-A (herein referred to as BCY17033); A-(SEQ ID NO: 83)-A (herein referred to as BCY17035); A-(SEQ ID NO: 84)-A (herein referred to as BCY17038); A-(SEQ ID NO: 85)-A (herein referred to as BCY17040); A-(SEQ ID NO: 86)-A (herein referred to as BCY17041); A-(SEQ ID NO: 87)-A (herein referred to as BCY17042); A-(SEQ ID NO: 88)-A (herein referred to as BCY17043); Ac-(SEQ ID NO: 89) (herein referred to as BCY19197); A-(SEQ ID NO: 90)-A (herein referred to as BCY16662); A-(SEQ ID NO: 91)-A (herein referred to as BCY16663); A-(SEQ ID NO: 91)-A-[Sar6]-[KFl] (herein referred to as BCY16639); A-(SEQ ID NO: 92)-A (herein referred to as BCY16664); A-(SEQ ID NO: 93)-A (herein referred to as BCY16665); A-(SEQ ID NO: 94)-A (herein referred to as BCY16666); A-(SEQ ID NO: 95)-A (herein referred to as BCY16667); A-(SEQ ID NO: 95)-A-[Sar6]-[KFl] (herein referred to as BCY16643); A-(SEQ ID NO: 95)-A-[K(PYA)] (herein referred to as BCY17238); Ac-(SEQ ID NO: 95) (herein referred to as BCY19193); A-(SEQ ID NO: 96)-A (herein referred to as BCY19192); Ac-(SEQ ID NO: 96) (herein referred to as BCY19196); Ac-(SEQ ID NO: 97) (herein referred to as BCY19194); Ac-(SEQ ID NO: 98) (herein referred to as BCY19195); Ac-(SEQ ID NO: 99) (herein referred to as BCY19198); Ac-(SEQ ID NO: 100) (herein referred to as BCY19199); Ac-(SEQ ID NO: 101) (herein referred to as BCY19200); Ac-(SEQ ID NO: 102) (herein referred to as BCY19203); Ac-(SEQ ID NO: 103) (herein referred to as BCY19205); Ac-(SEQ ID NO: 104) (herein referred to as BCY19206); A-(SEQ ID NO: 105)-A (herein referred to as BCY15208); A-(SEQ ID NO: 105)-A-[K(PYA)] (herein referred to as BCY15751); A-(SEQ ID NO: 106)-A-[K(PYA)] (herein referred to as BCY21608); A-(SEQ ID NO: 107)-A (herein referred to as BCY15209); A-(SEQ ID NO: 107)-A-[Sar6]-[KFl] (herein referred to as BCY15197); A-(SEQ ID NO: 108)-A (herein referred to as BCY15727); A-(SEQ ID NO: 108)-A-[K(PYA)] (herein referred to as BCY17452); Ac-(SEQ ID NO: 108)-[K(PYA)] (herein referred to as BCY19157); Ac-A-(SEQ ID NO: 108)-A-[K(PYA)] (herein referred to as BCY19158); A-(SEQ ID NO: 108)-A-[Sar6]-[(K(Ac)] (herein referred to as BCY19385); A-(SEQ ID NO: 108)-AGAA AE (herein referred to as BCY19580); A-(SEQ ID NO: 108)-KMTH E (herein referred to as BCY21192); A-(SEQ ID NO: 108)-NDSLN (herein referred to as BCY21193 ); A-(SEQ ID NO: 108)-SVNAN (herein referred to as BCY21194); A-(SEQ ID NO: 108)-QGH TPL (herein referred to as BCY21195); A-(SEQ ID NO: 108)-EMEH SN (herein referred to as BCY21196); MR Q-(SEQ ID NO: 108)-ETP (herein referred to as BCY21197); EHM-(SEQ ID NO: 108)-TQ S (herein referred to as BCY21198); EPKR Q-(SEQ ID NO: 108)-A (herein referred to as BCY21199); ANYA N-(SEQ ID NO: 108)-A (herein referred to as BCY21200); DSFH Q-(SEQ ID NO: 108)-A (herein referred to as BCY21201); MRQ-(SEQ ID NO: 108)-ETP-[K(PYA)] (herein referred to as BCY21993); EPKR Q-(SEQ ID NO: 108)-A-[K(PYA)] (herein referred to as BCY21994); Ac-(SEQ ID NO: 108)-A-[K(PYA)] (herein referred to as BCY23137); Ac-(SEQ ID NO: 108)-E-[K(PYA)] (herein referred to as BCY23174); A-(SEQ ID NO: 108)-E-[K(PYA)] (herein referred to as BCY23179); A-(SEQ ID NO: 109)-A-[K(PYA)] (herein referred to as BCY19159); A-(SEQ ID NO: 110)-A-[K(PYA)] (herein referred to as BCY19161); A-(SEQ ID NO: 111)-A-[K(PYA)] (herein referred to as BCY19162); A-(SEQ ID NO: 112)-A-[K(PYA)] (herein referred to as BCY19163); A-(SEQ ID NO: 113)-A-[K(PYA)] (herein referred to as BCY19164); A-(SEQ ID NO: 114)-A-[K(PYA)] (herein referred to as BCY19165); A-(SEQ ID NO: 115)-A-[K(PYA)] (herein referred to as BCY19166); A-(SEQ ID NO: 116)-A-[K(PYA)] (herein referred to as BCY19167); A-(SEQ ID NO: 117)-A (herein referred to as BCY19170); A-(SEQ ID NO: 117)-A-[K(PYA)] (herein referred to as BCY19284); Ac-(SEQ ID NO: 117)-[K(PYA)] (herein referred to as BCY19995); A-(SEQ ID NO: 118)-A-[K(PYA)] (herein referred to as BCY19171); A-(SEQ ID NO: 119)-A-[K(PYA)] (herein referred to as BCY19177); MRQ-(SEQ ID NO: 119)-ETP-[K(PYA)] (herein referred to as BCY21995); EPKR Q-(SEQ ID NO: 119)-A-[K(PYA)] (herein referred to as BCY21996); MRQ-(SEQ ID NO: 119)-ETP (herein referred to as BCY21997); EPKR Q-(SEQ ID NO: 119)-A (herein referred to as BCY21998); Ac-(SEQ ID NO: 119)-[K(PYA)] (herein referred to as BCY22499); A-(SEQ ID NO: 120)-A-[K(PYA)] (herein referred to as BCY19179); A-(SEQ ID NO: 121)-A-[K(PYA)] (herein referred to as BCY19181); A-(SEQ ID NO: 122)-A-[K(PYA)] (herein referred to as BCY19184); A-(SEQ ID NO: 123)-A-[K(PYA)] (herein referred to as BCY19185); A-(SEQ ID NO: 124)-A-[K(PYA)] (herein referred to as BCY19187); A-(SEQ ID NO: 125)-A-[K(PYA)] (herein referred to as BCY19188); A-(SEQ ID NO: 126)-A-[K(PYA)] (herein referred to as BCY19189); [dA]-(SEQ ID NO: 127)-[dA]-[K(PYA)] (herein referred to as BCY20840); A-(SEQ ID NO: 128)-A-[K(PYA)] (herein referred to as BCY21040); A-(SEQ ID NO: 129)-A (herein referred to as BCY21631); A-(SEQ ID NO: 129) (herein referred to as BCY21633); Ac-(SEQ ID NO: 129) (herein referred to as BCY21634); A-(SEQ ID NO: 130) (herein referred to as BCY21635); Ac-(SEQ ID NO: 130) (herein referred to as BCY21636); Ac-(SEQ ID NO: 131)-[K(PYA)] (herein referred to as BCY23702); Ac-(SEQ ID NO: 132)-[K(PYA)] (herein referred to as BCY23703); Ac-(SEQ ID NO: 132)-[K(PYA)-(Triazolyl)-(PEG)2-methyl] (herein referred to as BCY25601); Ac-(SEQ ID NO: 133)-[K(PYA)] (herein referred to as BCY23704); Ac-(SEQ ID NO: 134)-[K(PYA)] (herein referred to as BCY23705); Ac-(SEQ ID NO: 135)-[K(PYA)] (herein referred to as BCY23706); Ac-(SEQ ID NO: 136)-[K(PYA)] (herein referred to as BCY23707); Ac-(SEQ ID NO: 136)-[K(PYA)-(Triazolyl)-(PEG)2-methyl] (herein referred to as BCY25602); A-(SEQ ID NO: 137)-A (herein referred to as BCY15729); A-(SEQ ID NO: 138)-A (herein referred to as BCY15210); A-(SEQ ID NO: 138)-A-[Sar6] -[KFl] (herein referred to as BCY15198); A-(SEQ ID NO: 138)-A-[K(PYA)] (herein referred to as BCY15752); A-(SEQ ID NO: 139)-A (herein referred to as BCY15731); A-(SEQ ID NO: 139)-A-[Sar6] -[KFl] (herein referred to as BCY15730); A-(SEQ ID NO: 140)-A (herein referred to as BCY15733); A-(SEQ ID NO: 141)-A (herein referred to as BCY15735); and A-(SEQ ID NO: 141)-A-[Sar6] -[KFl] (herein referred to as BCY15734); or a modified derivative and / or pharmaceutically acceptable salt thereof. In a further embodiment, the molecular scaffold is a derivative of TATB which has the following structure: wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of X15-X16-X17-X18-X19-X20-X21-X22-X23-X24-X25-X26-X27-X28-X29(SEQ ID NO: 3) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 142)-A (herein referred to as BCY17001); A-(SEQ ID NO: 143)-A (herein referred to as BCY18128); A-(SEQ ID NO: 143)-A-[K(PYA)] (herein referred to as BCY19743); A-(SEQ ID NO: 144)-A (herein referred to as BCY18129); A-(SEQ ID NO: 144)-A-[K(PYA)] (herein referred to as BCY19744); Ac-A-(SEQ ID NO: 144)-A (herein referred to as BCY24131 ); Ac-(SEQ ID NO: 144) (herein referred to as BCY24135); A-(SEQ ID NO: 144) (herein referred to as BCY24450); Ac-A-(SEQ ID NO: 144) (herein referred to as BCY24451); (SEQ ID NO: 144)-A (herein referred to as BCY24452); Ac-(SEQ ID NO: 144)-A (herein referred to as BCY24453); AHG G-(SEQ ID NO: 144)-EVHA (herein referred to as BCY25863 ); AI KP-(SEQ ID NO: 144)-QHEA (herein referred to as BCY25864); ADST-(SEQ ID NO: 144)-QH PA (herein referred to as BCY25865); ALNG-(SEQ ID NO: 144)-PLS A (herein referred to as BCY25866); ALNG-(SEQ ID NO: 144)-PLS A-[K(PYA)] (herein referred to as BCY28840); A-(SEQ ID NO: 145)-A (herein referred to as BCY24442); A-(SEQ ID NO: 146)-A (herein referred to as BCY24443); A-(SEQ ID NO: 147)-A (herein referred to as BCY24444); A-(SEQ ID NO: 148)-A (herein referred to as BCY24445); A-(SEQ ID NO: 149)-A (herein referred to as BCY24456); A-(SEQ ID NO: 150)-A (herein referred to as BCY24457); A-(SEQ ID NO: 151)-A (herein referred to as BCY24458); A-(SEQ ID NO: 152)-A (herein referred to as BCY24459); A-(SEQ ID NO: 153)-A (herein referred to as BCY24462); A-(SEQ ID NO: 154)-A (herein referred to as BCY24466); A-(SEQ ID NO: 155)-A (herein referred to as BCY24467); A-(SEQ ID NO: 156)-A (herein referred to as BCY24468); A-(SEQ ID NO: 157)-A (herein referred to as BCY24469); A-(SEQ ID NO: 158)-A (herein referred to as BCY24471); A-(SEQ ID NO: 159)-A (herein referred to as BCY24472); A-(SEQ ID NO: 160)-A (herein referred to as BCY24473); A-(SEQ ID NO: 161)-A (herein referred to as BCY24474); A-(SEQ ID NO: 162)-A (herein referred to as BCY24475); A-(SEQ ID NO: 163)-A (herein referred to as BCY24477); A-(SEQ ID NO: 164)-A (herein referred to as BCY24478); A-(SEQ ID NO: 165)-A (herein referred to as BCY24479); A-(SEQ ID NO: 166)-A (herein referred to as BCY24480); A-(SEQ ID NO: 167)-A (herein referred to as BCY24481); A-(SEQ ID NO: 168)-A (herein referred to as BCY24482); A-(SEQ ID NO: 169)-A (herein referred to as BCY24483); A-(SEQ ID NO: 170)-A (herein referred to as BCY24484); A-(SEQ ID NO: 171)-A (herein referred to as BCY24485); A-(SEQ ID NO: 172)-A (herein referred to as BCY24486); A-(SEQ ID NO: 173)-A (herein referred to as BCY24487); A-(SEQ ID NO: 174)-A (herein referred to as BCY24488); A-(SEQ ID NO: 175)-A (herein referred to as BCY24489); A-(SEQ ID NO: 176)-A (herein referred to as BCY24490); A-(SEQ ID NO: 177)-A (herein referred to as BCY24491); A-(SEQ ID NO: 178)-A (herein referred to as BCY24492); A-(SEQ ID NO: 179)-A (herein referred to as BCY24493); A-(SEQ ID NO: 180)-A (herein referred to as BCY24495); A-(SEQ ID NO: 181)-A (herein referred to as BCY24496); A-(SEQ ID NO: 182)-A (herein referred to as BCY24497); A-(SEQ ID NO: 183)-A (herein referred to as BCY24498); A-(SEQ ID NO: 184)-A (herein referred to as BCY24499); A-(SEQ ID NO: 185)-A (herein referred to as BCY24500); A-(SEQ ID NO: 186)-A (herein referred to as BCY24501); A-(SEQ ID NO: 187)-A (herein referred to as BCY24503); A-(SEQ ID NO: 188)-A (herein referred to as BCY24504); A-(SEQ ID NO: 189)-A (herein referred to as BCY24505); A-(SEQ ID NO: 190)-A (herein referred to as BCY24506); A-(SEQ ID NO: 191)-A (herein referred to as BCY24509); ALNG-(SEQ ID NO: 192)-PLS A (herein referred to as BCY28838); ALNG-(SEQ ID NO: 192)-PLS A-[K(PYA)] (herein referred to as BCY28841); ALNG-(SEQ ID NO: 193)-PLS A (herein referred to as BCY28839); ALNG-(SEQ ID NO: 193)-PLS A-[K(PYA)] (herein referred to as BCY28842); ALEQ N-(SEQ ID NO: 194)-A (herein referred to as BCY25861); ALEQ N-(SEQ ID NO: 194)-A-[K(PYA)] (herein referred to as BCY28843); ALEQ N-(SEQ ID NO: 195)-A (herein referred to as BCY28844 ); ALEQ N-(SEQ ID NO: 195)-A-[K(PYA)] (herein referred to as BCY28845); and AHAG T-(SEQ ID NO: 196)-A (herein referred to as BCY25859 ); or a modified derivative and / or pharmaceutically acceptable salt thereof. In a further embodiment, the molecular scaffold is a derivative of TATB which has the following structure: wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of C-Q-P-T-X30-X31-C-X32-X33-X34-X35-X36-X37-C (SEQ ID NO: 4) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 197)-A (herein referred to as BCY16999); A-(SEQ ID NO: 197)-A-[K(PYA)] (herein referred to as BCY17693); A-(SEQ ID NO: 197)-A-[Sar6]-[K(Ac)] (herein referred to as BCY19387); A-(SEQ ID NO: 198)-A (herein referred to as BCY18126); Ac-A-(SEQ ID NO: 198)-A (herein referred to as BCY20725); A-(SEQ ID NO: 198)-NLNLK (herein referred to as BCY21770 ); VNEN I-(SEQ ID NO: 198)-A (herein referred to as BCY21771); A-(SEQ ID NO: 198)-RNPH D (herein referred to as BCY21772); A-(SEQ ID NO: 198)-IHN NG (herein referred to as BCY21774); TNEG I-(SEQ ID NO: 198)-A (herein referred to as BCY21778); VNEN I-(SEQ ID NO: 198)-A-[K(PYA)] (herein referred to as BCY23767); A-(SEQ ID NO: 199)-A (herein referred to as BCY20731); A-(SEQ ID NO: 200)-A (herein referred to as BCY20732); A-(SEQ ID NO: 201)-A (herein referred to as BCY20734); A-(SEQ ID NO: 202)-A (herein referred to as BCY20735); A-(SEQ ID NO: 203)-A (herein referred to as BCY20736); A-(SEQ ID NO: 204)-A (herein referred to as BCY20737); A-(SEQ ID NO: 205)-A (herein referred to as BCY20738); A-(SEQ ID NO: 206)-A (herein referred to as BCY20741); A-(SEQ ID NO: 207)-A (herein referred to as BCY20742); A-(SEQ ID NO: 208)-A (herein referred to as BCY20743); A-(SEQ ID NO: 209)-A (herein referred to as BCY20746); A-(SEQ ID NO: 210)-A (herein referred to as BCY20747); A-(SEQ ID NO: 211)-A (herein referred to as BCY20748); A-(SEQ ID NO: 212)-A (herein referred to as BCY20749); A-(SEQ ID NO: 213)-A (herein referred to as BCY20751); A-(SEQ ID NO: 214)-A (herein referred to as BCY20752); A-(SEQ ID NO: 215)-A (herein referred to as BCY20756); A-(SEQ ID NO: 216)-A (herein referred to as BCY20757); A-(SEQ ID NO: 217)-A (herein referred to as BCY20758); A-(SEQ ID NO: 218)-A (herein referred to as BCY20759); A-(SEQ ID NO: 219)-A (herein referred to as BCY20760); A-(SEQ ID NO: 220)-A (herein referred to as BCY20761); A-(SEQ ID NO: 221)-A (herein referred to as BCY20762); A-(SEQ ID NO: 222)-A (herein referred to as BCY20763); A-(SEQ ID NO: 223)-A (herein referred to as BCY20764); A-(SEQ ID NO: 224)-A (herein referred to as BCY20765); A-(SEQ ID NO: 225)-A (herein referred to as BCY20766); A-(SEQ ID NO: 226)-A (herein referred to as BCY18127); and A-(SEQ ID NO: 226)-A-[K(PYA)] (herein referred to as BCY19742); or a modified derivative and / or pharmaceutically acceptable salt thereof. In a further embodiment, the molecular scaffold is a tri-substituted 2,4,6-tris(bromomethyl)-s- triazine derivative of TBMT or TCTZ having the following structure: wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of C-Y-Y-X38-X39-X40-Y-A-C-L-D-C (SEQ ID NO: 5) additionally comprises N- and / or C- terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 227)-A (herein referred to as BCY17007); A-(SEQ ID NO: 228)-A (herein referred to as BCY18135); A-(SEQ ID NO: 229)-A (herein referred to as BCY18136); and A-(SEQ ID NO: 229)-A-[K(PYA)] (herein referred to as BCY19747); or a modified derivative and / or pharmaceutically acceptable salt thereof. In a further embodiment, the molecular scaffold is a derivative of TATA which has the following structure: wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of X41-X42-X43-X44-X45-X46-X47-X48-X49-C-X50-X51-X52-X53-X54(SEQ ID NO: 6) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 230)-A (herein referred to as BCY15211); A-(SEQ ID NO: 230)-A-[Sar6]-[KFl] (herein referred to as BCY15199); A-(SEQ ID NO: 231)-A (herein referred to as BCY15737); A-(SEQ ID NO: 232)-A (herein referred to as BCY15739); A-(SEQ ID NO: 232)-A-[Sar6]-[KFl] (herein referred to as BCY15738); A-(SEQ ID NO: 232)-A-[Sar6]-[K(Ac)] (herein referred to as BCY19386); A-(SEQ ID NO: 232)-AGAA AE (herein referred to as BCY19581); A-(SEQ ID NO: 233)-A (herein referred to as BCY17047); A-(SEQ ID NO: 234)-A (herein referred to as BCY17049); A-(SEQ ID NO: 235)-A (herein referred to as BCY17051); A-(SEQ ID NO: 236)-A (herein referred to as BCY17055); A-(SEQ ID NO: 237)-A (herein referred to as BCY17056); A-(SEQ ID NO: 238)-A (herein referred to as BCY17057); A-(SEQ ID NO: 239)-A (herein referred to as BCY17058); A-(SEQ ID NO: 240)-A (herein referred to as BCY17059); A-(SEQ ID NO: 241)-A (herein referred to as BCY17061); A-(SEQ ID NO: 242)-A (herein referred to as BCY17656); A-(SEQ ID NO: 243)-A (herein referred to as BCY15741); A-(SEQ ID NO: 244)-A (herein referred to as BCY15743); A-(SEQ ID NO: 245)-A (herein referred to as BCY15745); A-(SEQ ID NO: 246)-A (herein referred to as BCY16668); A-(SEQ ID NO: 247)-A (herein referred to as BCY16669); A-(SEQ ID NO: 248)-A (herein referred to as BCY16670); A-(SEQ ID NO: 249)-A (herein referred to as BCY16671); A-(SEQ ID NO: 249)-A-[Sar6]-[KFl] (herein referred to as BCY16647); Ac-A-(SEQ ID NO: 249)-A (herein referred to as BCY19586 ); A-(SEQ ID NO: 250)-A (herein referred to as BCY18510); A-(SEQ ID NO: 251)-A (herein referred to as BCY18511); A-(SEQ ID NO: 251)-A-[K(PYA)] (herein referred to as BCY25826); A-(SEQ ID NO: 252)-A (herein referred to as BCY18514); A-(SEQ ID NO: 253)-A (herein referred to as BCY18515); A-(SEQ ID NO: 254)-A (herein referred to as BCY18518); A-(SEQ ID NO: 255)-A (herein referred to as BCY18519); A-(SEQ ID NO: 256)-A (herein referred to as BCY18520); A-(SEQ ID NO: 257)-A (herein referred to as BCY16672); A-(SEQ ID NO: 258)-A (herein referred to as BCY16673); A-(SEQ ID NO: 258)-A-[Sar6]-[KFl] (herein referred to as BCY16649); A-(SEQ ID NO: 258)-A-[K(PYA)] (herein referred to as BCY17237); Ac-A-(SEQ ID NO: 258)-A (herein referred to as BCY19585); and A-(SEQ ID NO: 259)-A (herein referred to as BCY16674); or a modified derivative and / or pharmaceutically acceptable salt thereof. In a further embodiment, the molecular scaffold is a tri-substituted 2,4,6-tris(bromomethyl)-s- triazine derivative of TBMT or TCTZ having the following structure: wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of X41-X42-X43-X44-X45-X46-X47-X48-X49-C-X50-X51-X52-X53-X54(SEQ ID NO: 6) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 260)-A (herein referred to as BCY17002); A-(SEQ ID NO: 260)-A-[K(PYA)] (herein referred to as BCY19745); A-(SEQ ID NO: 261)-A (herein referred to as BCY18130); A-(SEQ ID NO: 261)-A-[K(PYA)] (herein referred to as BCY20847); [PYA]-A-(SEQ ID NO: 261)-A (herein referred to as BCY20852); Ac-(SEQ ID NO: 261) (herein referred to as BCY21616); A-(SEQ ID NO: 261) (herein referred to as BCY21617); Ac-A-(SEQ ID NO: 261) (herein referred to as BCY21618); [PYA]-(SEQ ID NO: 261) (herein referred to as BCY21619); [GuanAc]-(SEQ ID NO: 261)-A (herein referred to as BCY23043); A-(SEQ ID NO: 261)-[CF3Ala] (herein referred to as BCY23080); A-(SEQ ID NO: 261)-S (herein referred to as BCY23081); A-(SEQ ID NO: 262)-A (herein referred to as BCY20848); A-(SEQ ID NO: 263)-A (herein referred to as BCY20849); A-(SEQ ID NO: 264)-A (herein referred to as BCY20850); A-(SEQ ID NO: 265)-A (herein referred to as BCY20851); A-(SEQ ID NO: 266)-A (herein referred to as BCY20853); A-(SEQ ID NO: 266) (herein referred to as BCY21620); A-(SEQ ID NO: 267)-A (herein referred to as BCY21622); A-(SEQ ID NO: 267)-A-[K(PYA)] (herein referred to as BCY21607); Ac-(SEQ ID NO: 268) (herein referred to as BCY21624); A-(SEQ ID NO: 268) (herein referred to as BCY21625); [PYA]-(SEQ ID NO: 268) (herein referred to as BCY21626); A-(SEQ ID NO: 269) (herein referred to as BCY21627); Ac-(SEQ ID NO: 270) (herein referred to as BCY22879); Ac-(SEQ ID NO: 271) (herein referred to as BCY22880); A-(SEQ ID NO: 272)-A (herein referred to as BCY23044); A-(SEQ ID NO: 273)-A (herein referred to as BCY23045); A-(SEQ ID NO: 274)-A (herein referred to as BCY23046); A-(SEQ ID NO: 275)-A (herein referred to as BCY23047); A-(SEQ ID NO: 276)-A (herein referred to as BCY23050); A-(SEQ ID NO: 277)-A (herein referred to as BCY23051); A-(SEQ ID NO: 278)-A (herein referred to as BCY23052); A-(SEQ ID NO: 279)-A (herein referred to as BCY23053); A-(SEQ ID NO: 280)-A (herein referred to as BCY23054); A-(SEQ ID NO: 281)-A (herein referred to as BCY23058); A-(SEQ ID NO: 282)-A (herein referred to as BCY23059); A-(SEQ ID NO: 283)-A (herein referred to as BCY23062); A-(SEQ ID NO: 284)-A (herein referred to as BCY23063); A-(SEQ ID NO: 285)-A (herein referred to as BCY23064); A-(SEQ ID NO: 286)-A (herein referred to as BCY23066); A-(SEQ ID NO: 287)-A (herein referred to as BCY23067); A-(SEQ ID NO: 288)-A (herein referred to as BCY23068); A-(SEQ ID NO: 289)-A (herein referred to as BCY23071); A-(SEQ ID NO: 290)-A (herein referred to as BCY23072); A-(SEQ ID NO: 291)-A (herein referred to as BCY23073); A-(SEQ ID NO: 292)-A (herein referred to as BCY23074); A-(SEQ ID NO: 293)-A (herein referred to as BCY23075); A-(SEQ ID NO: 294)-A (herein referred to as BCY23079); [GuanAc]-(SEQ ID NO: 295)-COOH (herein referred to as BCY27058); [GuanAc]-(SEQ ID NO: 295) (herein referred to as BCY27059); [CIA]-[K(PYA)]-(SEQ ID NO: 295)-A (herein referred to as BCY27064); [CIA]-[dK(PYA)]-(SEQ ID NO: 295)-A (herein referred to as BCY27065); [GuanAc]-(SEQ ID NO: 296) (herein referred to as BCY27060); [GuanAc]-(SEQ ID NO: 297) (herein referred to as BCY27061); [GuanAc]-(SEQ ID NO: 298) (herein referred to as BCY27062); [GuanAc]-(SEQ ID NO: 299) (herein referred to as BCY27063); [GuanAc]-(SEQ ID NO: 300) (herein referred to as BCY27066); [GuanAc]-(SEQ ID NO: 301) (herein referred to as BCY27067); [GuanAc]-(SEQ ID NO: 302) (herein referred to as BCY27068); A-(SEQ ID NO: 303)-A (herein referred to as BCY18131); A-(SEQ ID NO: 304)-A (herein referred to as BCY18132); A-(SEQ ID NO: 305)-A-[K(PYA)] (herein referred to as BCY19588); A-(SEQ ID NO: 306)-A (herein referred to as BCY19933); A-(SEQ ID NO: 307)-A (herein referred to as BCY19934); A-(SEQ ID NO: 308)-A (herein referred to as BCY19935); A-(SEQ ID NO: 309)-A (herein referred to as BCY19936); A-(SEQ ID NO: 309)-A-[K(PYA)] (herein referred to as BCY21606); Ac-(SEQ ID NO: 309) (herein referred to as BCY23139); Ac-A-(SEQ ID NO: 309)-A (herein referred to as BCY23140); [dA]-(SEQ ID NO: 309)-A (herein referred to as BCY32061); A-(SEQ ID NO: 309) (herein referred to as BCY32074); Ac-A-(SEQ ID NO: 309) (herein referred to as BCY32075); (SEQ ID NO: 309)-A (herein referred to as BCY32076); Ac-(SEQ ID NO: 309)-A (herein referred to as BCY32077); A-(SEQ ID NO: 309)-A-[dK(PYA)] (herein referred to as BCY32126); A-(SEQ ID NO: 309)-[K(PYA)] (herein referred to as BCY32127); A-(SEQ ID NO: 309)-[dK(PYA)] (herein referred to as BCY32128); A-(SEQ ID NO: 310)-A (herein referred to as BCY23138); A-(SEQ ID NO: 310)-A-[K(PYA)] (herein referred to as BCY24613); A-(SEQ ID NO: 311)-A (herein referred to as BCY32062); A-(SEQ ID NO: 312)-A (herein referred to as BCY32065); A-(SEQ ID NO: 313)-A (herein referred to as BCY32066); A-(SEQ ID NO: 314)-A (herein referred to as BCY32069); A-(SEQ ID NO: 315)-A (herein referred to as BCY32071); A-(SEQ ID NO: 316)-A (herein referred to as BCY32072); A-(SEQ ID NO: 317)-A (herein referred to as BCY32078); A-(SEQ ID NO: 318)-A (herein referred to as BCY32079); A-(SEQ ID NO: 319)-A (herein referred to as BCY32080); A-(SEQ ID NO: 320)-A (herein referred to as BCY32081); A-(SEQ ID NO: 321)-A (herein referred to as BCY32082); A-(SEQ ID NO: 322)-A (herein referred to as BCY32083); A-(SEQ ID NO: 323)-A (herein referred to as BCY32084); A-(SEQ ID NO: 324)-A (herein referred to as BCY32085); A-(SEQ ID NO: 325)-A (herein referred to as BCY32086); A-(SEQ ID NO: 326)-A (herein referred to as BCY32087); A-(SEQ ID NO: 327)-A (herein referred to as BCY32088); A-(SEQ ID NO: 328)-A (herein referred to as BCY32089); A-(SEQ ID NO: 329)-A (herein referred to as BCY32090); A-(SEQ ID NO: 330)-A (herein referred to as BCY32091); A-(SEQ ID NO: 331)-A (herein referred to as BCY32092); A-(SEQ ID NO: 332)-A (herein referred to as BCY32093); A-(SEQ ID NO: 333)-A (herein referred to as BCY32095); A-(SEQ ID NO: 334)-A (herein referred to as BCY32096); A-(SEQ ID NO: 335)-A (herein referred to as BCY32098); A-(SEQ ID NO: 336)-A (herein referred to as BCY32099); A-(SEQ ID NO: 337)-A (herein referred to as BCY32100); A-(SEQ ID NO: 338)-A (herein referred to as BCY32101); A-(SEQ ID NO: 339)-A (herein referred to as BCY32103); A-(SEQ ID NO: 340)-A (herein referred to as BCY32104); A-(SEQ ID NO: 341)-A (herein referred to as BCY32105); A-(SEQ ID NO: 342)-A (herein referred to as BCY32106); A-(SEQ ID NO: 343)-A (herein referred to as BCY32107); A-(SEQ ID NO: 344)-A (herein referred to as BCY32108); A-(SEQ ID NO: 345)-A (herein referred to as BCY32109); A-(SEQ ID NO: 346)-A (herein referred to as BCY32110); A-(SEQ ID NO: 347)-A (herein referred to as BCY32112); A-(SEQ ID NO: 348)-A (herein referred to as BCY32113); A-(SEQ ID NO: 349)-A (herein referred to as BCY32114); A-(SEQ ID NO: 350)-A (herein referred to as BCY32115); A-(SEQ ID NO: 351)-A (herein referred to as BCY32116); A-(SEQ ID NO: 352)-A (herein referred to as BCY32117); A-(SEQ ID NO: 353)-A (herein referred to as BCY32120); A-(SEQ ID NO: 354)-A (herein referred to as BCY32121); A-(SEQ ID NO: 355)-A (herein referred to as BCY32122); A-(SEQ ID NO: 356)-A (herein referred to as BCY32123); A-(SEQ ID NO: 357)-A (herein referred to as BCY32124); A-(SEQ ID NO: 358)-A (herein referred to as BCY32125); A-(SEQ ID NO: 359)-A (herein referred to as BCY19937); A-(SEQ ID NO: 360)-A (herein referred to as BCY19938); A-(SEQ ID NO: 361)-A (herein referred to as BCY19939); A-(SEQ ID NO: 362)-A (herein referred to as BCY19940); A-(SEQ ID NO: 363)-A (herein referred to as BCY19941); A-(SEQ ID NO: 364)-A (herein referred to as BCY19942); A-(SEQ ID NO: 365)-A (herein referred to as BCY19943); and A-(SEQ ID NO: 366)-A (herein referred to as BCY18253); or a modified derivative and / or pharmaceutically acceptable salt thereof. Multimeric Binding Complexes According to a further aspect of the invention, there is provided a multimeric binding complex which comprises at least two bicyclic peptide ligands (for example, 2, 3, or 4 bicyclic peptide ligands), which may be the same or different, wherein at least one bicyclic peptide ligand is a peptide ligand as defined herein, or a pharmaceutically acceptable salt thereof. According to a further aspect of the invention, there is provided a multimeric binding complex which comprises at least two bicyclic peptide ligands as defined herein, wherein said peptide ligands may be the same or different, or a pharmaceutically acceptable salt thereof. In some embodiments the multimeric binding complex comprises for example, 2, 3, or 4 bicyclic peptide ligands as defined herein, wherein said peptide ligands may be the same or different. In one embodiment, the multimeric binding complexes comprise more than one bicyclic peptide which are the same (i.e. homomultimers). In an alternative embodiment, the multimeric binding complexes comprise bicyclic peptides which are different (i.e. heteromultimers). In one embodiment the multimeric binding complex comprises at least two bicycle peptide ligands which are the same and at least one different bicycle peptide. In some embodiments the multimeric binding complex comprises (a) two bicycle peptide ligands which are the same and (b) one or two further bicycle peptide ligands which may be the same or different, and wherein the two further bicycle peptide ligands of (b) may be the same or different to the two bicycle peptide ligands of (a). In one embodiment the multimeric binding complex additional comprises one or more effector groups and / or functional groups, such as one or more cytotoxic agents, radiochelators or chromophores. The effector and / or functional group may also be which produces a detectable signal in the presence of a second intermediate (for example, biotin and various protein antigens). For biotin, the secondary intermediate may include streptavidin-enzyme conjugates or streptavidin-dye conjugates. In one embodiment, the multimeric binding complex additionally comprises a fluorophore. Spacers In one embodiment, the multimeric binding complex additionally comprises a spacer or hinge moiety, or one or more spacers or hinge moieties. Such a spacer or hinge moiety is configured to hold the multiple bicyclic peptide ligands in an optimal arrangement for presentation to the target. It will be appreciated that the bicyclic peptide ligands in a multimeric binding complex may be conjugated to each other via any suitable linker. The term linker is used interchangeably herein with spacer and hinge moiety. The properties of the linker may be modulated to increase length, rigidity or solubility to optimise the desired functional outcome. Increasing the valency of either binding peptide may serve to increase the affinity of the heteromultimer for the target. In one embodiment the linker is a linear linker or a branched linker. In some embodiments the linker is a branched linker and comprises three or four branches. In some embodiments the linker is capable of binding to three or four bicyclic peptide ligands. In some embodiments the linker comprises three branches and is capable of binding to three bicyclic peptide ligands. In some embodiments the linker comprises four branches and is capable of binding to four bicyclic peptide ligands. In some embodiments the linker comprises one or more repeating monomer groups. In some embodiments, the linker is a bidentate or polydentate group having a length of from about 0.3 nm to about 300 nm. In some embodiments the linker has a length of from about 0.5 nm to about 200 nm, such as from about 1 nm to about 100 nm, e.g. from about 1.5 nm to about 50 nm, e.g. from about 2 nm to about 20 nm, such as from about 3 nm to about 10 nm. In some embodiments the linker length is the persistence length. In some embodiments the length is determined when linker is in aqueous solution under physiological conditions, (e.g. phosphate buffered saline, pH 7.4 at 37 °C) and in some embodiments can be determined using atomic force microscopy. In some embodiments, the linker comprises one or more linking moieties such as one or more poly(alkyleneglycol) groups such as poly(ethyleneglycol) or poly(propyleneglycol). In some embodiments the linker may comprise one or more groups such as an amine group, an amide group; an alkylene group; a carbamate group; an ether group; an ester group; a disulphide bond; a hydrazone group; a sulfonamide group; a thioether group; or a cyclic group, preferably a 4-12 membered carbocyclic or heterocyclic group, a 5-12 membered heteroaryl group or a C6-12aryl group; wherein said alkylene, alkenylene, alkynylene, poly(alkyleneglycol), amine and cyclic group is each independently optionally substituted. In some embodiments the linker comprises one or more amino acids or amino acid analogs. In some embodiments the linker comprises from about 1 to about 5 amino acids or amino acid analogs. In some embodiments the side chains of two amino acids or amino acid analogs in the linker are attached together. In some embodiments the linker comprises a moiety of form wherein each R1is H or C1-4alkyl; each R2is selected from the side chain of an amino acid (e.g. a canonical amino acid) or is C1-4 alkyl which may be substituted e.g. with OH, SH, SC1-4 alkyl, aryl (which may be substituted with OH), heteroaryl, C(O)OH, C(O)NH2, N+H3, NH(C=N+H2)NH2, for example, R2may comprise the side chain of arginine or homo-arginine; and wherein LINK is a linker, wherein LINK is optionally a C2-8 hydrocarbylene (e.g. alkylene) linker optionally terminated by or substituted with one or more groups such as an amine group, an amide group; an alkylene group; a carbamate group; an ether group; an ester group; a disulphide bond; a hydrazone group; a sulfonamide group; a thioether group; or a cyclic group as defined herein; for example, LINK may comprise a C3-6alkylene group which terminates in or is interrupted by an amide group; e.g. LINK may comprise a moiety of form -C1-4alkylene-NHC(O)-C1-4alkylene-, e.g. -C4alkylene-NHC(O)-C1alkylene-. In some embodiments said moiety is attached to a polypeptide comprised in a peptide ligand or bicyclic peptide ligand as defined herein, e.g. at the N- or C- terminus of a polypeptide comprised in a peptide ligand or bicyclic peptide ligand as defined herein. In some embodiments the linker comprises one or more reactive groups for reaction with a bicyclic peptide ligand as described herein. Exemplary reactive groups include azide groups (which may react with alkyne groups on a bicyclic peptide ligand as described herein, e.g. in the presence of suitable conditions, for example in the presence of an azide-alkyne cycloaddition catalyst, e.g. thereby forming a 1,2,3-triazole group); carboxylic acids and activated derivatives thereof (such as NHS-esters) (which may react with amine groups on a bicyclic peptide ligand as described herein, e.g. in the presence of suitable conditions, e.g. thereby forming an amide bond), and the like. In the bicyclic peptide ligands described herein, WKH^WHUPV^³D]LGH´^DQG^³WULD]RO\O´^DUH^VRPHWLPHV^XVHG^LQWHUFKDQJHDEO\^WR^GHVFULEH^WKH^VDPH^ VWUXFWXUH^^ZKHUH^³D]LGH´^UHIHUV^WR^WKH^VWUXFWXUH^Iound in the linker prior to conjugation to the ELF\FOLF^SHSWLGH^ OLJDQG^^DQG^³WULD]RO\O´^ UHIHUV^ WR^ WKH^VWUXFWXUH^IRXQG^ LQ^WKH^OLQNHU^ZKHQ^ LW^KDV^ reacted with an alkynyl group on the bicyclic peptide ligand. In some embodiments when the linker comprises a poly(alkyleneglycol), the poly(alkyleneglycol) is poly(ethyleneglycol) (PEG) or poly(propyleneglycol) (PPG). In some embodiments the linker comprises one or more group PEGn, wherein n represents the number of contiguous ethyleneglycol units in each said PEG group. In some embodiments n is an integer from about 1 to about 30, such as about 2 to about 25, or about 3 to about 10. In some embodiments the linker comprises one or more branches e.g. three branches and each branch comprises a PEGngroup. In some embodiments when the linker comprises an amide group, said amide group is of formula -NHC(O)- or -C(O)NH-. In some embodiments when the linker comprises an amine group, the amine group is of formula N(R)3, wherein each R may be the same or different. In some embodiments each R comprises a bicyclic peptide ligand as described herein, for example attached to the amine nitrogen via a linking moiety comprising one or more group PEGnas described herein. In some embodiments when the linker comprises a cyclic group the cyclic group is a C6aryl group. In some embodiments when the linker comprises an alkylene group the alkylene group is a C1-3alkylene group. Linkers as described above may also be used to conjugate the bicyclic peptide ligand(s) to an effector group and / or functional group as defined herein. Typically, a linker which conjugates an effector and / or functional group to the bicyclic peptide ligand(s) comprises or consists of one or more group PEGn, wherein n represents the number of contiguous ethyleneglycol units in each said PEG group. In some embodiments n is an integer from about 1 to about 30, such as about 2 to about 25, or about 3 to about 10. In some embodiments, a linker which conjugates an effector and / or functional group to the bicyclic peptide ligand(s) is a covalent bond. Dimers In one embodiment, the multimeric binding complex comprises two bicyclic peptides which are either the same (i.e. homodimers) or different (i.e. heterodimers). In one embodiment, the multimeric binding complex comprises two bicyclic peptides which are the same (i.e. homodimers). In one embodiment, the multimeric binding complex comprises two bicyclic peptides which are different (i.e. heterodimers). When the multimeric binding complex comprises two bicyclic peptides, it will be appreciated that the spacer will require 2 points of attachment. In some embodiments of a dimer, the linker is a group of formula N3í(Alk1)míPEGní(Alk1)míNHC(O)(Alk2^&^2^1+í^$ON1)míPEGní(Alk1)míN3wherein each Alk1is independently a C1-3alkylene group; Alk2is a C1-6alkylene group; each m is independently 0 or 1; n is an integer from about 1 to about 30; and wherein Alk2is optionally substituted with a functional group capable of forming a linker to an effector and / or functional group as defined herein, for example a fluorophore. In some embodiments, Alk2is a C5 alkylene group. In some embodiments, Alk2 LV^í&+2CH2CH(N*H)CH2CH2í, wherein * is the point of connection to an effector and / or functional group as defined herein, optionally wherein Alk2is conjugated to said effector and / or functional group via a linker. In some embodiments, Alk2LV^í&+2CH2CH(NH(fluorophore))CH2CH2í, wherein fluorophore is a fluorophore as defined herein, for example AlexaFluor488. An example of such a linker is ³$+'$-(PEG10-N3^´^^ZKLFK^LV^&RPSRXQG^^^LQ^([DPSOH^^^ In some embodiments of a dimer, the linker is a group of formula N3í(Alk1)míPEGní(Alk1)míNHC(O)(Alk2)&^2^1+í^$ON1)míPEGní(Alk1)míN3wherein each Alk1is independently a C1-3alkylene group; Alk2is a C1-6alkylene group; each m is independently 0 or 1; n is an integer from about 1 to about 30. In some embodiments, Alk2is a propylene group. In some embodiments, where Alk2is a propylene group, such a OLQNHU^PD\^EH^UHIHUUHG^WR^DV^³*7$-Pegn-N3´^^IRU^H[DPSOH^³*7$-PEG10-N3´^DV^VKRZQ^LQ^ Examples 5 and 6 which describe the synthesis of BCY26427 and BCY26435. In some embodiments of a dimer, the linker is a group of formula [N3²(Alk)m²PEGn²(Alk)m-]2-N-[-(Alk)m²PEGn²(Alk)m²Z] wherein each Alk is independently a C1-3alkylene group which independently optionally terminates in an amide group or an -O- group; each m is independently 0, 1 or 2; each n is independently an integer from about 1 to about 30; and Z comprises an effector and / or functional group as defined herein. In some embodiments, Z is or comprises biotin. In some embodiments, Z is or comprises a fluorophore as defined herein, for example Bodipy558. For avoidance of doubt, each group [N3²(Alk)m²PEGn²(Alk)m-] may be the same or different. In some embodiments of a dimer, the linker is a group of formula N3²(Alk)m²PEGn²(Alk)m²Q wherein each Alk is independently a C1-3alkylene group which independently optionally terminates in an amide group or an -O- group; each m is independently 0 or 1; n is an integer from about 1 to about 30; and Q is a carboxylic acid (C(O)OH) or activated derivative thereof (e.g. an NHS-ester group). In one embodiment, the multimeric binding complex comprises two bicyclic peptides and the multimeric binding complex is a motif of formula (A) or formula (B): ZKHUHLQ^%&<^UHSUHVHQWV^WKH^³bicyclic peptide ligand. As explained above, those skilled in the art will appreciate that the triazolyl groups displayed in the structures above arise from the reaction between an azide group in the linker with an alkyne group on the bicyclic peptide ligand (e.g. to an alkyne group comprised in a K(PYA) moiety as described herein). In one embodiment, the multimeric binding complex comprises a dimeric binding complex described in the following Table 1: Table 1: Exemplified Dimeric Binding Complexes of the Invention Multimer Composition Compound Number BCY16282 AF488-AHDA-(amido-Peg10-triazolyl)[BCY15751]2 BCY26427 GTA-[amido-Peg10-triazolyl]2[BCY25826]2 BCY26435 GTA-[amido-Peg10-triazolyl]2[BCY24613]2 BCY28218 N-(Biotin-PEG23]-N-bis(PEG3-azide)[BCY24613]2 BCY28219 N-(Biotin-PEG23]-N-bis(PEG3-azide)[BCY21996]2 BCY28220 N-(Biotin-PEG23]-N-bis(PEG3-azide)[BCY25826]2 BCY28885 N-(Biotin-PEG23]-N-bis(PEG3-azide)[BCYBCY19741]2 BCY28887 N-(Biotin-PEG23]-N-bis(PEG3-azide)[BCY19743]2 BCY28222 N-(Biotin-PEG10)-N-bis(PEG10-azide)[BCY23767]2 BCY28223 N-(Biotin-PEG10)-N-bis(PEG10-azide)[BCY24613]2 BCY28224 N-(Biotin-PEG10)-N-bis(PEG10-azide)[BCY21996]2 BCY28225 N-(Biotin-PEG10)-N-bis(PEG10-azide)[BCY25826]2 BCY28886 N-(Biotin-PEG10)-N-bis(PEG10-azide)[BCY19741]2 BCY28888 N-(Biotin-PEG10)-N-bis(PEG10-azide)[BCY19743]2 BCY26436 GTA-[amido-Peg23-triazolyl]2[BCY24613]2 BCY31478 N-(amine-PEG10)-[BDP558-N3SC2]-N-bis(PEG10-azide)[BCY24613]2 BCY34406 N-(acid-PEG10)-[BDP558-N3SC1]-N-bis(PEG10-azide)[BCY24613]2 wherein AF488 represents AlexaFluor488; AHDA is derived from the name of the compound AHDA-[Peg10-N3]2(Compound 4 in Example 2), GTA refers to glutaric anhydride (but which ring opens when used in the linkers to form a -C(O)(CH2)5C(O)- moiety, BDP558 represents For example, the structure of BCY26427 is:

[0002] In some embodiments, the multimeric binding complex is selected from BCY28218, BCY28219, BCY28220, BCY28885, BCY28887, or a pharmaceutically acceptable salt thereof. In some embodiments, the multimeric binding complex is BCY26435, or a pharmaceutically acceptable salt thereof. Trimers In one embodiment, the multimeric binding complex comprises three bicyclic peptides which are either the same (i.e. homotrimers) or different (i.e. heterotrimers). In a further embodiment, the heterotrimer comprises one bicyclic peptide of a first sequence and two bicyclic peptides of a second sequence. In one embodiment, the multimeric binding complex comprises three bicyclic peptides which are the same. In some embodiments of a trimer, the linker is a group of formula [N3²(Alk)m²PEGn²(Alk)m-]3-N wherein each Alk is independently a C1-3alkylene group which independently optionally terminates in an amide group or an -O- group; each m is independently 0, 1 or 2; each n is independently an integer from about 1 to about 30. For avoidance of doubt, each [N3² (Alk)m²PEGn²(Alk)m-] may be the same or different. When the multimeric binding complex comprises three bicyclic peptides, it will be appreciated that the spacer will require 3 points of attachment. Thus, in one embodiment, the multimeric binding complex comprises three bicyclic peptides and the multimeric binding complex is a motif of formula (C) or formula (D): (C),

[0003] (D), wherein BCY represents the bicyclic peptide ligand. In one embodiment, the multimeric binding complex comprises a trimeric binding complex described in the following Table 2: Table 2: Exemplified Trimeric Binding Complexes of the Invention Multimer Composition Compound Number BCY25832 TCA-[amido-Peg10-triazolyl]3[BCY25826]3 BCY26437 TCA-[amido-Peg10-triazolyl]3[BCY24613]3 BCY28283 TCA-[amido-Peg5-triazolyl]3[BCY20840]3 BCY26442 TCA-[amido-Peg23-triazolyl]3[BCY24613]3 wherein TCA is N((CH2)2O(CH2)2CONH)3.Tetramers In one embodiment, the multimeric binding complex comprises four bicyclic peptides which are either the same (i.e. homotetramers) or different (i.e. heterotetramers). In a further embodiment, the heterotetramer comprises one bicyclic peptide of a first sequence and three bicyclic peptides of a second sequence. In an alternative embodiment, the heterotetramer comprises two bicyclic peptides of a first sequence and two bicyclic peptides of a second sequence. In one embodiment, the multimeric binding complex comprises four bicyclic peptides which are the same. In some embodiments of a tetramer, the linker is a group of formula [N3²(Alk)m²PEGn²(Alk)m-]4-C wherein each Alk is independently a C1-3alkylene group which independently optionally terminates in an amide group or an -O- group; each m is independently 0, 1 or 2; each n is independently an integer from about 1 to about 30. For avoidance of doubt, each [N3² (Alk)m²PEGn²(Alk)m-] may be the same or different. When the multimeric binding complex comprises four bicyclic peptides, it will be appreciated that the spacer will require 4 points of attachment. Thus, in one embodiment, the multimeric binding complex comprises four bicyclic peptides and the multimeric binding complex is a motif wherein BCY represents the bicyclic peptide ligand. In one embodiment, the multimeric binding complex comprises a tetrameric binding complex described in the following Table 3: Table 3: Exemplified Tetrameric Binding Complexes of the Invention Multimer Composition Compound Number BCY15926 TET-[amido-Peg23-triazolyl]4[BCY15751]4 BCY25831 TET-[amido-Peg10-triazolyl]4[BCY25826]4 BCY26438 TET-[amido-Peg5-triazolyl]4[BCY24613]4 BCY26439 TET-[amido-Peg10-triazolyl]4[BCY24613]4 BCY21835 TET-[amido-Peg23-triazolyl]4[BCY20840]4 BCY21481 TET-[amido-Peg23-triazolyl]4[BCY19177]4 BCY21483 TET-[amido-Peg23-triazolyl]4[BCY21040]4 BCY29425 TET-[amido-Peg5-triazolyl]4[BCY23706]4 BCY29427 TET-[amido-Peg23-triazolyl]4[BCY23706]4 BCY28229 TET-[amido-Peg5-triazolyl]4[BCY21996]4 BCY28230 TET-[amido-Peg10-triazolyl]4[BCY21996]4 BCY26433 TET-[amido-Peg10-triazolyl]4[BCY23767]4 BCY26432 TET-[amido-Peg5-triazolyl]4[BCY23767]4 BCY28884 TET-[amido-Peg5-triazolyl]4[BCY19743]4 BCY30493 TET-[amido-Peg5-triazolyl]4[BCY28840]4 BCY30494 TET-[amido-Peg10-triazolyl]4[BCY28840]4 BCY30502 TET-[amido-Peg5-triazolyl]4[BCY28841]4 BCY30503 TET-[amido-Peg10-triazolyl]4[BCY28841]4 BCY30504 TET-[amido-Peg23-triazolyl]4[BCY28841]4 BCY26428 TET-[amido-Peg5-triazolyl]4[BCY25826]4 BCY25828 TET-[amido-Peg23-triazolyl]4[BCY25826]4 BCY26440 TET-[amido-Peg23-triazolyl]4[BCY24613]4 BCY26434 TET-[amido-Peg23-triazolyl]4[BCY23767]4 BCY29426 TET-[amido-Peg10-triazolyl]4[BCY23706]4 BCY28883 TET-[amido-Peg5-triazolyl]4[BCY19741]4 wherein TET is C((CH2)O(CH2)2CONH)4.As explained above, those skilled in the art will appreciate that when conjugated with bicyclic peptide ligands as described herein, the or each azide group will typically react with an alkyne group on one bicyclic peptide ligand (e.g. to an alkyne group comprised in a K(PYA) moiety as described herein, to form a triazolyl group). Any of the compounds identified above may be provided in the form of a pharmaceutically acceptable salt, also provided herein. Unless defined otherwise, all technical and scientific terms used herein have the same meaning as commonly understood by those of ordinary skill in the art, such as in the arts of peptide chemistry, cell culture and phage display, nucleic acid chemistry and biochemistry. Standard techniques are used for molecular biology, genetic and biochemical methods (see Sambrook et al., Molecular Cloning: A Laboratory Manual, 3rd ed., 2001, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY; Ausubel et al., Short Protocols in Molecular Biology (1999) 4thed., John Wiley & Sons, Inc.), which are incorporated herein by reference. Numbering When referring to amino acid residue positions within peptides of the invention, invariant residues are omitted from the numbering, therefore, the numbering of amino acid residues within peptides of the invention is referred to as below: C-X1-X2-X3-C-X4-X5-X6-X7-X8-X9-C (SEQ ID NO: 1). Molecular Format N- or C-terminal extensions to the bicycle core sequence are added to the left or right side of the sequence, separated by a hyphen. For example, an N-WHUPLQDO^ȕ$OD-Sar10-Ala tail would be denoted as: ȕAla-Sar10-A-(SEQ ID NO: X). ZKHUHLQ^6DU^UHSUHVHQWV^VDUFRVLQH^^DQG^ȕ$OD^UHSUHVHQWV^ȕ-Alanine. It will be appreciated that, unless specified otherwise, all bicyclic peptides have a C-terminal CONH2group with the exception of those which contain a C-terminal Cysam group (i.e. SEQ ID NO: 130) which lack said C-terminal CONH2group. In addition, in certain bicyclic peptides the C-terminal CONH2group may be replaced with a COOH group as shown herein for BCY27058. Inversed Peptide Sequences In light of the disclosure in Nair et al (2003) J Immunol 170(3), 1362-1373, it is envisaged that the peptide sequences disclosed herein would also find utility in their retro-inverso form. For example, the sequence is reversed (i.e. N-terminus becomes C-terminus and vice versa) and their stereochemistry is likewise also reversed (i.e. D-amino acids become L-amino acids and vice versa). Bicyclic Peptide Ligands A bicyclic peptide ligand, as referred to herein, refers to a peptide ligand covalently bound to a molecular scaffold. Typically, such bicyclic peptides comprise a polypeptide having natural or non-natural amino acids, two or more reactive groups (e.g. cysteine, homocysteine (hCys, (S)-2-Amino-4-VXOIDQ\OEXWDQRLF^ DFLG^^^ ȕ&\V^ ^^5^-3-amino-3-mercaptopropanoic acid), cysteamine (Cystam) or penicillamine (Pen, (R)-2-amino-3-mercapto-3-methylbutanoic acid), Dap ((S)-2,3-diaminopropanoic acid) or N-alkyl-Dap (e.g. N-methyl-Dap, (S)-2-amino-3- (methylamino)propanoic acid) which are capable of forming covalent bonds to the scaffold, and a sequence subtended between said reactive groups which is referred to as the loop sequence, since it forms a loop when the peptide is bound to the scaffold. In the present case, the peptides typically comprise at least three cysteine residues (for example, three cysteine residues), or two cysteine residues and one Cystam residue, and form at least two loops on the scaffold, most typically two loops. Accordingly, in some embodiments the present disclosure provides a peptide, a peptide ligand or a bicyclic peptide ligand as provided herein, wherein one or more of the cysteine or cysteamine residues of one or more of the polypeptides comprised in said peptide, peptide OLJDQG^^RU^ELF\FOLF^SHSWLGH^OLJDQG^LV^UHSODFHG^ZLWK^KRPRF\VWHLQH^^K&\V^^^ȕ&\V^ penicillamine (Pen), Dap or N-methyl-Dap. For avoidance of doubt, in the complexes provided herein which comprise two or more peptide ligands (e.g. two or more bicyclic peptide ligands), each said ligand is independently optionally modified in this way, such that different ligands may be modified or not and different modified ligands may comprise different modifications. Peptide specificity As explained above, in some embodiments the provided peptides and ligands comprising such (described in more detail herein) are specific for TLR3. In some embodiments the provided complexes (e.g. multimeric binding complexes) contain peptides and ligands comprising such (described in more detail herein) that are specific for TLR3. $V^XVHG^KHUHLQ^^WKH^WHUP^³VSHFLILF´^^³VSHFLILF^ELQGLQJ´^^HWF^^UHIHUV^LQ^LWV^EURDGHVW^ sense to a peptide or peptide ligand which binds to its biological target. In some embodiments the peptide or peptide ligand binds to its biological target in a specific manner; that is, the binding to the biological target is not non-specific. In some embodiments a peptide which exhibits non-specific binding is promiscuous; that is the peptide is capable of binding to multiple different biological species, typically including the target of interest and off-target binding sites, such as binding sites on cell types other than a target cell type. Accordingly, in some embodiments a peptide or peptide ligand which is chosen or designed to bind specifically to its intended target does not exhibit promiscuous binding to off-target binding sites. In some embodiments the binding to the target is a binding to a particular epitope on the target. A peptide or peptide ligand may be designed to be specific for a particular epitope or may be identified by suitable screening methods, such as display techniques (e.g. phage display) which can be used to develop high-affinity binders against given targets (e.g. epitopes). Alternatively, a peptide or peptide ligand can be identified with specific binding to a biological target (such as a cellular target) without knowledge of the specific epitope to which it binds. In some embodiments a peptide or peptide ligand which specifically binds to a target or epitope has a high affinity for the target or epitope. In some embodiments the binding affinity of a peptide or peptide ligand to its epitope may be expressed in terms of its dissociation constant (KD, also written as Kd). Typically, a peptide or peptide ligand which specifically binds to a biological target will have a KDagainst that target of less than 10 μM, e.g. less than 1 μM. Often, a peptide or peptide ligand which specifically binds to a biological target will have a nanomolar KDagainst that target, such as less than 500 nM, less than 250 nM, less than 100 nM, less than 20 nM, less than 10 nM or even less than 1 nM. Binding affinities can be determined by methods known in the art, such as SPR and competition assays. Some suitable assays are described in the examples. In some embodiments a peptide or peptide ligand which specifically binds to a biological target will have a higher affinity (lower KD) for the specific biological target than for other biological binding epitopes. For example, a peptide or peptide ligand which specifically binds to TLR3 will typically bind to TLR3 with a higher affinity than to other epitopes, for example other toll like receptors. In some embodiments a peptide or peptide ligand which specifically binds to a biological target will bind to the target with an affinity at least twice as strong, e.g. at least 5 times, e.g. at least 10 times, e.g. at least 20 time, e.g. at least 50 times, e.g. at least 100 times, e.g. at least 1000 times or more as strong as the binding of the peptide to any other off-target binding partners. Advantages of the Bicyclic Peptide Ligands Certain bicyclic peptides of the present invention have a number of advantageous properties which enable them to be considered as suitable drug-like molecules for injection, inhalation, nasal, ocular, oral or topical administration. Such advantageous properties include: -Species cross-reactivity. This is a typical requirement for preclinical pharmacodynamics and pharmacokinetic evaluation; -Protease stability. Bicyclic peptide ligands should ideally demonstrate stability to plasma proteases, epithelial ("membrane-anchored") proteases, gastric and intestinal proteases, lung surface proteases, intracellular proteases and the like. Protease stability should be maintained between different species such that a bicycle lead candidate can be developed in animal models as well as administered with confidence to humans; -Desirable solubility profile. This is a function of the proportion of charged and hydrophilic versus hydrophobic residues and intra / inter-molecular H-bonding, which is important for formulation and absorption purposes; -An optimal plasma half-life in the circulation. Depending upon the clinical indication and treatment regimen, it may be required to develop a bicyclic peptide for short exposure in an acute illness management setting, or develop a bicyclic peptide with enhanced retention in the circulation, and is therefore optimal for the management of more chronic disease states. Other factors driving the desirable plasma half-life are requirements of sustained exposure for maximal therapeutic efficiency versus the accompanying toxicology due to sustained exposure of the agent; and -Selectivity. Abbreviations A number of non-natural amino acids are utilised in the peptide ligands of the invention and for clarity they are referred to herein as abbreviations which are fully defined as follows: Agb: 2-amino-4-guanidinobutyric acid Aib: aminoisobutyric acid AlloIle: alloisoleucine Arg(Me): d-N methyl arginine AzaTrp: azatryptophan Aze: azetidine Cba: ȕ-cyclobutylalanine Cbg: cyclobutyl glycine CF3Ala: ȕ-trifluoromethylalanine CF3Nva:5,5,5-trifluoronorvaline (or (S)-2-amino-5,5,5-trifluoropentanoic acid) 4CF3Phe: 4-trifluoromethylphenylalanine C5g: cyclopentyl glycine CIA: carboximidamide Cis-HyP: cis-L-4-hydroxyproline Cit: citrulline 6ClTrp: 6-chloro-tryptophan Cysam: cysteamine Dap: diaminopropionic acid 44DFP: 4,4-difluoroproline 26DiMeTyr: 2,6-dimethyltyrosine DOPA: 3,4-dihydroxy-phenylalanine EPA: 2-amino-3-ethyl-pentanoic acid 4FlPro: 4-fluoro-proline 2FPhe: 2-fluoro-phenylalanine 3FPhe: 3-fluoro-phenylalanine 4FPhe: 4-fluoro-phenylalanine 4FTrp: 4-fluoro-L-tryptophan 5FTrp: 5-fluoro-L-tryptophan 6FTrp: 6-fluoro-L-tryptophan 7FTrp: 7-fluoro-L-tryptophan 2FTyr: 2-fluoro-tyrosine 3FTyr: 3-fluoro-tyrosine Gla: L-Ȗ-carboxyglutamic acid HArg: homoarginine His1Me: N1-methyl-L-histidine His3Me: N3-methyl-L-histidine HLeu: homoleucine HSer: homoserine HyP: hydroxyproline 3HyV: 3-hydroxy-L-valine KFl: lysine-fluorescein K(PYA): lysine, İ-4-pentynoyl 4MeOTrp: 4-methoxy-tryptophan 5MeOTrp: 5-methoxy-tryptophan 2MePhe: 2-methyl-phenylalanine 3MePhe: 3-methyl-phenylalanine 4MePhe: 4-methyl-phenylalanine 2MeTrp: 2-methyl-tryptophan 4MeTrp: 4-methyl-tryptophan 5MeTrp: 5-methyl-tryptophan 6MeTrp: 6-methyl-tryptophan 7MeTrp: 7-methyl-tryptophan 1Nal: 1-naphthylalanine 2Nal: 2-naphthylalanine Nle: norleucine Nva: norvaline Orn: ornithine PG: propargylglycine Pip: pipecolic acid PYA: pentynoic acid R-aMeLys(PYA): (R)-Į-methyllysine^^İ-4-pentynoyl S-aMeLys(PYA): (S)-Į-PHWK\OO\VLQH^^İ-4-pentynoyl tBuAla: t-butyl-alanine tBuGly: t-butyl-glycine 4tBuPhe: 4-t-butyl-phenylalanine 3tBuTyr: 3-t-butyl-tyrosine TfNle: 6,6,6-trifluoronorleucine trans-4FlPro: trans-4-fluoro-pyrrolidine-2-carboxylic acid Trp(Me): methyl-tryptophan Trp(S): Į-amino-benzo[b]thiophene-3-propanoic acid Pharmaceutically Acceptable Salts It will be appreciated that salt forms are within the scope of this invention, and references to peptide ligands include the salt forms of said ligands. The salts of the present invention can be synthesized from the parent compound that contains a basic or acidic moiety by conventional chemical methods such as methods described in Pharmaceutical Salts: Properties, Selection, and Use, P. Heinrich Stahl (Editor), Camille G. Wermuth (Editor), ISBN: 3-90639-026-8, Hardcover, 388 pages, August 2002. Generally, such salts can be prepared by reacting the free acid or base forms of these compounds with the appropriate base or acid in water or in an organic solvent, or in a mixture of the two. Acid addition salts (mono- or di-salts) may be formed with a wide variety of acids, both inorganic and organic. Examples of acid addition salts include mono- or di-salts formed with an acid selected from the group consisting of acetic, 2,2-dichloroacetic, adipic, alginic, ascorbic (e.g. L-ascorbic), L-aspartic, benzenesulfonic, benzoic, 4-acetamidobenzoic, butanoic, (+) camphoric, camphor-sulfonic, (+)-(1S)-camphor-10-sulfonic, capric, caproic, caprylic, cinnamic, citric, cyclamic, dodecylsulfuric, ethane-1,2-disulfonic, ethanesulfonic, 2- hydroxyethanesulfonic, formic, fumaric, galactaric, gentisic, glucoheptonic, D-gluconic, glucuronic (e.g. D-glucuronic), glutamic (e.g. L-JOXWDPLF^^^ Į-oxoglutaric, glycolic, hippuric, hydrohalic acids (e.g. hydrobromic, hydrochloric, hydriodic), isethionic, lactic (e.g. (+)-L-lactic, (±)-DL-lactic), lactobionic, maleic, malic, (-)-L-malic, malonic, (±)-DL-mandelic, methanesulfonic, naphthalene-2-sulfonic, naphthalene-1,5-disulfonic, 1-hydroxy-2-naphthoic, nicotinic, nitric, oleic, orotic, oxalic, palmitic, pamoic, phosphoric, propionic, pyruvic, L- pyroglutamic, salicylic, 4-amino-salicylic, sebacic, stearic, succinic, sulfuric, tannic, (+)-L- tartaric, thiocyanic, p-toluenesulfonic, undecylenic and valeric acids, as well as acylated amino acids and cation exchange resins. One particular group of salts consists of salts formed from acetic, hydrochloric, hydriodic, phosphoric, nitric, sulfuric, citric, lactic, succinic, maleic, malic, isethionic, fumaric, benzenesulfonic, toluenesulfonic, sulfuric, methanesulfonic (mesylate), ethanesulfonic, naphthalenesulfonic, valeric, propanoic, butanoic, malonic, glucuronic and lactobionic acids. One particular salt is the hydrochloride salt. Another particular salt is the acetate salt. If the compound is anionic, or has a functional group which may be anionic (e.g., -COOH may be -COO-), then a salt may be formed with an organic or inorganic base, generating a suitable cation. Examples of suitable inorganic cations include, but are not limited to, alkali metal ions such as Li+, Na+and K+, alkaline earth metal cations such as Ca2+and Mg2+, and other cations such as Al3+or Zn+. Examples of suitable organic cations include, but are not limited to, ammonium ion (i.e., NH4+) and substituted ammonium ions (e.g., NH3R+, NH2R2+, NHR3+, NR4+). Examples of some suitable substituted ammonium ions are those derived from: methylamine, ethylamine, diethylamine, propylamine, dicyclohexylamine, triethylamine, butylamine, ethylenediamine, ethanolamine, diethanolamine, piperazine, benzylamine, phenylbenzylamine, choline, meglumine, and tromethamine, as well as amino acids, such as lysine and arginine. An example of a common quaternary ammonium ion is N(CH3)4+. Where the peptides of the invention contain an amine function, these may form quaternary ammonium salts, for example by reaction with an alkylating agent according to methods well known to the skilled person. Such quaternary ammonium compounds are within the scope of the peptides of the invention. The peptides (including peptide ligands and complexes thereof) of the invention may exist as a zwitterion. Such compounds may also be provided in the form of a pharmaceutically acceptable salt. Suitable salts include those formed with pharmaceutically acceptable acids, which provide a proton to a negatively charged group such as a COO- group, and a counter- ion to balance the positive charge on a positively charged group such as a quaternary nitrogen atom. Suitable pharmaceutically acceptable acids include hydrochloric acid, sulphonic acids including methanesulphonic acid and toluene sulphonic acid, ascorbic acid and citric acid. Hydrochloric acid and sulphonic acids are preferred, in particular hydrochloric acid. Alternatively, zwitterions can be combined with pharmaceutically acceptable bases, for example, alkali metal (e.g. sodium or potassium) and alkali earth metal (e.g. calcium or magnesium) hydroxides. Modified Derivatives It will be appreciated that modified derivatives of the peptide ligands as defined herein are within the scope of the present invention. In some embodiments, modified derivatives include functional fragments, derivatives and variants of sequences provided herein. As those skilled in the art will appreciate, fragments of amino acid sequences include deletion variants of such sequences wherein one or more, such as at least 1, 2, 3, 4 or 5 amino acids are deleted. Deletion may occur at the C- terminus or N-terminus of the reference sequence or within the reference sequence. Derivatives of amino acid sequences include modified sequences including sequences which are modified in vivo or ex vivo. Many different protein modifications are known to those skilled in the art and include modifications to introduce new functionalities to amino acid residues, modifications to protect reactive amino acid residues or modifications to couple amino acid residues to chemical moieties such as reactive functional groups on linkers for attachment to such amino acid residues. Exemplary modifications that can be made to the provided peptides, ligands and related complexes are described in more detail herein. Derivatives of amino acid sequences include addition variants of such sequences wherein one or more, such as at least 1, 2, 3, 4, or 5 amino acids are added or introduced into the reference sequence. Addition may occur at the C- terminus or N-terminus of the reference sequence or within the reference sequence. Variants of amino acid sequences include sequences wherein one or more amino acid such as at least 1, 2, 3, 4, or 5 amino acid residues in the reference sequence are exchanged for one or more alternative residues. Variants of amino acid sequences include sequences carrying naturally occurring amino acids and / or unnatural amino acids. Variants, derivatives and fragments of the aforementioned amino acid sequences typically retain at least some of the activity / functionality of the reference sequence. In a preferred embodiment, the variants, derivatives and fragments substantially retain their biological function(s) as described herein. Thus, in one embodiment the variants, derivatives and fragments retain the binding specificity of the reference sequence i.e. the ability to specifically bind to TLR3. In one such embodiment, the variants, derivatives and fragments bind to the same epitope as the reference sequence. In another embodiment, the variants, derivatives and fragments retain the binding affinity of the reference sequence. Preferably, variants, derivatives and fragments of a reference sequence have increased / improved activity / functionality when compared to the reference sequence. In some embodiments a variant, derivative or fragment of an amino acid sequence is expressed in terms of its percentage identity to the reference sequence. Protocols to determine percent identity are routine procedures within the scope of those skilled in the art. Suitable methods include CLUSTAL W (Thompson et al., Nucleic Acids Research, 22(22) 4673-4680 (1994)) and iterative refinement (Gotoh, J. Mol. Biol.264(4) 823-838 (1996)); and methods described by Altschul et al., Bull. Math. Bio. 48: 603-16, 1986 and Henikoff and Henikoff, Proc. Natl. Acad. Sci. USA 89:10915-19, 1992. In an exemplary method, two amino acid sequences are aligned to optimize the alignment scores using a gap opening penalty of 10, a gap extension penalty of 1, and the "blosum 62" scoring matrix of Henikoff and Henikoff (ibid.), with percentage identity then calculated as: [100 x (T / L)]; wherein T = total number of identical matches and L = length of the longer sequence plus the number of gaps introduced into the longer sequence in order to align the two sequences. In some embodiments a variant, derivative or fragment of a reference sequence has at least at least 60% identity to the reference sequence, such as at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or more identity to the reference sequence. Examples of such suitable modified derivatives include one or more modifications selected from: N-terminal and / or C-terminal modifications; replacement of one or more amino acid residues with one or more non-natural amino acid residues or vice versa, replacement of one or more amino acids (e.g. one or more natural amino acids) with one or more isosteric and / or isolectronic amino acids, replacement of one or more natural amino acids with one or more isosteric and / or isoelectronic non-natural amino acids, or vice versa (such as replacement of one or more polar amino acid residues with one or more isosteric or isoelectronic amino acids; replacement of one or more non-polar amino acid residues with other non-natural isosteric or isoelectronic amino acids); addition of a spacer group; replacement of one or more oxidation sensitive amino acid residues with one or more oxidation resistant amino acid residues; replacement of one or more amino acid residues with an alanine, replacement of one or more L-amino acid residues with one or more D-amino acid residues; N-alkylation of one or more amide bonds within the bicyclic peptide ligand; replacement of one or more peptide bonds with a surrogate bond; peptide backbone length modification; substitution of the hydrogen on the alpha-carbon of one or more amino acid residues with another chemical group, modification of amino acids such as cysteine, lysine, glutamate / aspartate and tyrosine with suitable amine, thiol, carboxylic acid and phenol- reactive reagents so as to functionalise said amino acids, and introduction or replacement of amino acids that introduce orthogonal reactivities that are suitable for functionalisation, for example azide or alkyne-group bearing amino acids that allow functionalisation with alkyne or azide-bearing moieties, respectively. Amino acid residues may typically be replaced with other amino acid residues of similar chemical structure, similar chemical properties or similar side-chain volume ^³FRQVHUYDWLYH^ VXEVWLWXWLRQV´^. The amino acids introduced may have similar polarity, hydrophilicity, hydrophobicity, basicity, acidity, neutrality or charge to the amino acids they replace. Alternatively, the conservative substitution may introduce another amino acid that is aromatic or aliphatic in the place of a pre-existing aromatic or aliphatic amino acid. Conservative amino acid changes are well-known in the art and may be selected in accordance with the properties of the 20 main amino acids as defined in Table A above. Where amino acids have similar polarity, this can also be determined by reference to the hydropathy scale for amino acid side chains, which is well-known the person skilled in the art. In one embodiment, the modified derivative comprises an N-terminal and / or C-terminal modification. In a further embodiment, wherein the modified derivative comprises an N- terminal modification using suitable amino-reactive chemistry, and / or C-terminal modification using suitable carboxy-reactive chemistry. In a further embodiment, said N-terminal or C- terminal modification comprises addition of an effector group, including but not limited to a cytotoxic agent, a radiochelator or a chromophore. In a further embodiment, the modified derivative comprises an N-terminal modification. In a further embodiment, the N-terminal modification comprises an N-terminal acetyl group. In this embodiment, the N-terminal cysteine group is capped with acetic anhydride or other appropriate reagents during peptide synthesis leading to a molecule which is N-terminally acetylated. This embodiment provides the advantage of removing a potential recognition point for aminopeptidases and avoids the potential for degradation of the bicyclic peptide. In an alternative embodiment, the N-terminal modification comprises the addition of a molecular spacer group which facilitates the conjugation of effector groups and retention of potency of the bicyclic peptide to its target. In a further embodiment, the modified derivative comprises a C-terminal modification. In a further embodiment, the C-terminal modification comprises an amide group. In this embodiment, the C-terminal cysteine group is synthesized as an amide during peptide synthesis leading to a molecule which is C-terminally amidated. This embodiment provides the advantage of removing a potential recognition point for carboxypeptidase and reduces the potential for proteolytic degradation of the bicyclic peptide. In one embodiment, the modified derivative comprises replacement of one or more amino acid residues with one or more non-natural amino acid residues. In this embodiment, non-natural amino acids may be selected having isosteric / isoelectronic side chains which are neither recognised by degradative proteases nor have any adverse effect upon target potency. Alternatively, non-natural amino acids may be used having constrained amino acid side chains, such that proteolytic hydrolysis of the nearby peptide bond is conformationally and sterically impeded. In particular, these concern proline analogues, bulky sidechains, CD- disubstituted derivatives (for example, aminoisobutyric acid, Aib), and cyclo amino acids, a simple derivative being amino-cyclopropylcarboxylic acid. In one embodiment, the modified derivative comprises the addition of a spacer group. In a further embodiment, the modified derivative comprises the addition of a spacer group to the N-terminal cysteine and / or the C-terminal cysteine. In one embodiment, the modified derivative comprises replacement of one or more oxidation sensitive amino acid residues with one or more oxidation resistant amino acid residues. In one embodiment, the modified derivative comprises replacement of one or more charged amino acid residues with one or more hydrophobic amino acid residues. In an alternative embodiment, the modified derivative comprises replacement of one or more hydrophobic amino acid residues with one or more charged amino acid residues. The correct balance of charged versus hydrophobic amino acid residues is an important characteristic of the bicyclic peptide ligands. For example, hydrophobic amino acid residues influence the degree of plasma protein binding and thus the concentration of the free available fraction in plasma, while charged amino acid residues (in particular arginine) may influence the interaction of the peptide with the phospholipid membranes on cell surfaces. The two in combination may influence half-life, volume of distribution and exposure of the peptide drug, and can be tailored according to the clinical endpoint. In addition, the correct combination and number of charged versus hydrophobic amino acid residues may reduce irritation at the injection site (if the peptide drug has been administered subcutaneously). In one embodiment, the modified derivative comprises replacement of one or more L-amino acid residues with one or more D-amino acid residues. This embodiment is believed to increase proteolytic stability by steric hindrance and by a propensity of D-amino acids to stabilise E-turn conformations (Tugyi et al (2005) PNAS, 102(2), 413±418). In one embodiment, the modified derivative comprises removal of any amino acid residues and substitution with alanines. This embodiment provides the advantage of removing potential proteolytic attack site(s). It should be noted that each of the above-mentioned modifications serve to deliberately improve the potency or stability of the peptide. Further potency improvements based on modifications may be achieved through the following mechanisms: -Incorporating hydrophobic moieties that exploit the hydrophobic effect and lead to lower off rates, such that higher affinities are achieved; -Incorporating charged groups that exploit long-range ionic interactions, leading to faster on rates and to higher affinities (see for example Schreiber et al, Rapid, electrostatically assisted association of proteins (1996), Nature Struct. Biol.3, 427-31); and -Incorporating additional constraint into the peptide, by for example constraining side chains of amino acids correctly such that loss in entropy is minimal upon target binding, constraining the torsional angles of the backbone such that loss in entropy is minimal upon target binding and introducing additional cyclisations in the molecule for identical reasons. (for reviews see Gentilucci et al, Curr. Pharmaceutical Design, (2010), 16, 3185-203, and Nestor et al, Curr. Medicinal Chem (2009), 16, 4399-418). Isotopic Variations The present invention includes all pharmaceutically acceptable (radio)isotope-labeled peptide ligands of the invention, wherein one or more atoms are replaced by atoms having the same atomic number, but an atomic mass or mass number different from the atomic mass or mass number usually found in nature, and peptide ligands of the invention, wherein metal chelating JURXSV^DUH^DWWDFKHG^^WHUPHG^³HIIHFWRU´^^WKDW^DUH^FDSDEOH^RI^KROGLQJ^UHOHYDQW^^UDGLR^LVRWRSHV^^ and peptide ligands of the invention, wherein certain functional groups are covalently replaced with relevant (radio)isotopes or isotopically labelled functional groups. Examples of isotopes suitable for inclusion in the peptide ligands of the invention comprise isotopes of hydrogen, such as2H (D) and3H (T), carbon, such as11C,13C and14C, chlorine, such as36Cl, fluorine, such as18F, iodine, such as123I,125I and131I, nitrogen, such as13N and15N, oxygen, such as15O,17O and18O, phosphorus, such as32P, sulfur, such as35S, copper, such as64Cu, gallium, such as67Ga or68Ga, yttrium, such as90Y and lutetium, such as177Lu, and Bismuth, such as213Bi. Certain isotopically-labelled peptide ligands of the invention, for example, those incorporating a radioactive isotope, are useful in drug and / or substrate tissue distribution studies. The peptide ligands of the invention can further have valuable diagnostic properties in that they can be used for detecting or identifying the formation of a complex between a labelled compound and other molecules, peptides, proteins, enzymes or receptors. The detecting or identifying methods can use compounds that are labelled with labelling agents such as radioisotopes, enzymes, fluorescent substances, luminous substances (for example, luminol, luminol derivatives, luciferin, aequorin and luciferase), etc. The radioactive isotopes tritium, i.e.3H (T), and carbon-14, i.e.14C, are particularly useful for this purpose in view of their ease of incorporation and ready means of detection. Substitution with heavier isotopes such as deuterium, i.e.2H (D), may afford certain therapeutic advantages resulting from greater metabolic stability, for example, increased in vivo half-life or reduced dosage requirements, and hence may be preferred in some circumstances. Substitution with positron emitting isotopes, such as11C,18F,15O and13N, can be useful in Positron Emission Topography (PET) studies for examining target occupancy. Isotopically-labeled compounds of peptide ligands of the invention can generally be prepared by conventional techniques known to those skilled in the art or by processes analogous to those described in the accompanying Examples using an appropriate isotopically-labeled reagent in place of the non-labeled reagent previously employed. Molecular Scaffold In some embodiments a polypeptide disclosed herein is attached to a molecular scaffold. In one embodiment, the molecular scaffold comprises a non-aromatic molecular scaffold. 5HIHUHQFHV^KHUHLQ^ WR^³QRQ-aromatic moleculDU^VFDIIROG´^ UHIHUV^WR^DQ\^PROHFXODU^VFDIIROG^DV^ defined herein which does not contain an aromatic (i.e. unsaturated) carbocyclic or heterocyclic ring system. Accordingly, in some embodiments the polypeptide is attached to a non-aromatic molecular scaffold. In other embodiments the polypeptide is attached to an aromatic molecular scaffold. Molecular scaffolds are described in, for example, WO 2009 / 098450 and references cited therein, particularly WO 2004 / 077062 and WO 2006 / 078161. As noted in the foregoing documents, the molecular scaffold may be a small molecule, such as a small organic molecule. In one embodiment the molecular scaffold may be a macromolecule. In one embodiment the molecular scaffold is a macromolecule composed of amino acids, nucleotides or carbohydrates. In one embodiment the molecular scaffold comprises reactive groups that are capable of reacting with functional group(s) of the polypeptide to form covalent bonds. The molecular scaffold may comprise chemical groups which form the linkage with a peptide, such as amines, thiols, alcohols, ketones, aldehydes, nitriles, carboxylic acids, esters, alkenes, alkynes, azides, anhydrides, succinimides, maleimides, alkyl halides and acyl halides. The molecular scaffold of the invention contains chemical groups that allow functional groups of the polypeptide of the encoded library of the invention to form covalent links with the molecular scaffold. Said chemical groups are selected from a wide range of functionalities including amines, thiols, alcohols, ketones, aldehydes, nitriles, carboxylic acids, esters, alkenes, alkynes, anhydrides, succinimides, maleimides, azides, alkyl halides and acyl halides. Scaffold reactive groups that could be used on the molecular scaffold to react with thiol groups of cysteines are alkyl halides (or also named halogenoalkanes or haloalkanes). Examples include bromomethylbenzene or iodoacetamide. Other scaffold reactive groups that are used to selectively couple compounds to cysteines in proteins are maleimides, DE unsaturated carbonyl containing compounds and D^halomethylcarbonyl containing compounds. Examples of maleimides which may be used as molecular scaffolds in the invention include: tris-(2-maleimidoethyl)amine, tris-(2-maleimidoethyl)benzene, tris- (maleimido)benzene. In one embodiment, the molecular scaffold is selected from 1,1',1''-(1,3,5-triazinane-1,3,5- triyl)triprop-2-en-1-one (also known as triacryloylhexahydro-s-triazine; TATA), 1,3,5- tris(bromoacetyl) hexahydro-1,3,5-triazine (TATB), 2,4,6-tris(bromomethyl)-s-triazine (TBMT), and 2,4,6-tris(chloromethyl)-1,3,5-triazine (TCTZ). In a further embodiment, the molecular scaffold is 1,1',1''-(1,3,5-triazinane-1,3,5-triyl)triprop- 2-en-1-one (also known as triacryloylhexahydro-s-triazine (TATA)): TATA. Thus, following cyclisation with the bicyclic peptides of the invention (e.g.) on the cysteine residues, the molecular scaffold forms a tri-substituted 1,1',1''-(1,3,5-triazinane-1,3,5- triyl)tripropan-1-one derivative of TATA having the following structure: , which may also be depicted as , wherein * denotes the point of attachment of the three cysteine residues. In an alternative embodiment, the molecular scaffold is 1,3,5-tris(bromoacetyl) hexahydro-1, 3,5-triazine (TATB): Thus, following cyclisation with the bicyclic peptides of the invention on (e.g.) the cysteine residues, the molecular scaffold forms a tri-substituted 1,3,5-tris(bromoacetyl) hexahydro-1,3, 5-triazine derivative of TATB having the following structure: which may also be depicted as wherein * denotes the point of attachment of the three cysteine residues. In an alternative embodiment, the molecular scaffold is 2,4,6-tris(bromomethyl)-s-triazine (TBMT): TBMT. Thus, following cyclisation with the bicyclic peptides of the invention on the Ci, Cii, and Ciiicysteine residues, the molecular scaffold forms a tri-substituted 2,4,6-tris(bromomethyl)-s- triazine derivative of TBMT having the following structure: which may also be depicted as wherein * denotes the point of attachment of the (e.g.) three cysteine residues. Full details of TBMT and derivatisation are its use in cyclic peptides are described in van de Langemheen et al (2016) ChemBioChem 10.1002 / cbic.201600612 In an alternative embodiment, the molecular scaffold is 2,4,6-tris(chloromethyl)-1,3,5-triazine (TCTZ): TCTZ. Thus, following cyclisation with the bicyclic peptides of the invention on the Ci, Cii, and Ciiicysteine residues, the molecular scaffold forms a tri-substituted 2,4,6-tris(chloromethyl)-s- triazine derivative of TCTZ having the following structure: wherein * denotes the point of attachment of the (e.g.) three cysteine residues. It will be appreciated that, following cyclisation of the bicyclic peptides of the invention with either TBMT or TCTZ, the derivatives of TBMT and TCTZ which form the molecular scaffold have the same structure, as represented above. Therefore, where reference is made herein to a molecular scaffold which is a derivative of TBMT, the molecular scaffold may also be a derivative of TCTZ. Reactive Groups The molecular scaffold of the invention may be bonded to the polypeptide via functional or reactive groups on the polypeptide. These are typically formed from the side chains of particular amino acids found in the polypeptide polymer. Such reactive groups may be a cysteine side chain, a homocysteine side chain (hCys, (S)-2-Amino-4-sulfanylbutanoic acid), D^ȕ&\V^VLGH^FKDLQ^^^5^-3-amino-3-mercaptopropanoic acid), a cysteamine side chain (Cysam, 2-Aminoethanethiol), a penicillamine side chain (Pen, (R)-2-amino-3-mercapto-3- methylbutanoic acid), a Dap group ((S)-2,3-diaminopropanoic acid), a N-alkyl-Dap group (e.g. N-methyl-Dap, (S)-2-amino-3-(methylamino)propanoic acid, a [Dap(Me)] group, a lysine side chain, or an N-terminal amine group or any other suitable reactive group. Details may be found in WO 2009 / 098450. In one embodiment, the reactive groups are all cysteine residues. Examples of reactive groups of natural amino acids are the thiol group of cysteine, the amino group of lysine, the carboxyl group of aspartate or glutamate, the guanidinium group of arginine, the phenolic group of tyrosine or the hydroxyl group of serine. Non-natural amino acids can provide a wide range of reactive groups including an azide, a keto-carbonyl, an alkyne, a vinyl, or an aryl halide group. The amino and carboxyl group of the termini of the polypeptide can also serve as reactive groups to form covalent bonds to a molecular scaffold / molecular core. The polypeptides of the invention contain at least three reactive groups. Said polypeptides can also contain four or more reactive groups. The more reactive groups are used, the more loops can be formed in the molecular scaffold. In a preferred embodiment, polypeptides with three reactive groups are generated. Reaction of said polypeptides with a molecular scaffold / molecular core having a three-fold rotational symmetry generates a single product isomer. The generation of a single product isomer is favourable for several reasons. The nucleic acids of the compound libraries encode only the primary sequences of the polypeptide but not the isomeric state of the molecules that are formed upon reaction of the polypeptide with the molecular core. If only one product isomer can be formed, the assignment of the nucleic acid to the product isomer is clearly defined. If multiple product isomers are formed, the nucleic acid cannot give information about the nature of the product isomer that was isolated in a screening or selection process. The formation of a single product isomer is also advantageous if a specific member of a library of the invention is synthesized. In this case, the chemical reaction of the polypeptide with the molecular scaffold yields a single product isomer rather than a mixture of isomers. In another embodiment of the invention, polypeptides with four reactive groups are generated. Reaction of said polypeptides with a molecular scaffold / molecular core having a tetrahedral symmetry generates two product isomers. Even though the two different product isomers are encoded by one and the same nucleic acid, the isomeric nature of the isolated isomer can be determined by chemically synthesizing both isomers, separating the two isomers and testing both isomers for binding to a target ligand. In one embodiment of the invention, at least one of the reactive groups of the polypeptides is orthogonal to the remaining reactive groups. The use of orthogonal reactive groups allows the directing of said orthogonal reactive groups to specific sites of the molecular core. Linking strategies involving orthogonal reactive groups may be used to limit the number of product isomers formed. In other words, by choosing distinct or different reactive groups for one or more of the at least three bonds to those chosen for the remainder of the at least three bonds, a particular order of bonding or directing of specific reactive groups of the polypeptide to specific positions on the molecular scaffold may be usefully achieved. In another embodiment, the reactive groups of the polypeptide of the invention are reacted with molecular linkers wherein said linkers are capable to react with a molecular scaffold so that the linker will intervene between the molecular scaffold and the polypeptide in the final bonded state. In some embodiments, amino acids of the members of the libraries or sets of polypeptides can be replaced by any natural or non-natural amino acid. Excluded from these exchangeable amino acids are the ones harbouring functional groups for cross-linking the polypeptides to a molecular core, such that the loop sequences alone are exchangeable. The exchangeable polypeptide sequences have either random sequences, constant sequences or sequences with random and constant amino acids. The amino acids with reactive groups are either located in defined positions within the polypeptide, since the position of these amino acids determines loop size. In one embodiment, a polypeptide with three reactive groups has the sequence (X)lY(X)mY(X)nY(X)o, wherein Y represents an amino acid with a reactive group, X represents a random amino acid, m and n are numbers between 2 and 8 defining the length of intervening polypeptide segments, which may be the same or different, and l and o are numbers between 0 and 20 defining the length of flanking polypeptide segments. Alternatives to thiol-mediated conjugations can be used to attach the molecular scaffold to the peptide via covalent interactions. Alternatively, these techniques may be used in modification or attachment of further moieties (such as small molecules of interest which are distinct from the molecular scaffold) to the polypeptide after they have been selected or isolated according to the present invention ± in this embodiment then clearly the attachment need not be covalent and may embrace non-covalent attachment. These methods may be used instead of (or in combination with) the thiol mediated methods by producing phage that display proteins and peptides bearing unnatural amino acids with the requisite chemical reactive groups, in combination small molecules that bear the complementary reactive group, or by incorporating the unnatural amino acids into a chemically or recombinantly synthesised polypeptide when the molecule is being made after the selection / isolation phase. Further details can be found in WO 2009 / 098450 or Heinis, et al., Nat Chem Biol 2009, 5 (7), 502-7. Effector and Functional Groups According to a further aspect of the invention, there is provided a drug conjugate comprising a peptide ligand, bicyclic peptide ligand or multimeric binding complex as described herein, conjugated to one or more effector and / or functional groups. Effector and / or functional groups can be attached, for example, to the N and / or C termini of the polypeptide, to an amino acid within the polypeptide, or to the molecular scaffold. Appropriate effector groups include antibodies and parts or fragments thereof. For instance, an effector group can include an antibody light chain constant region (CL), an antibody CH1 heavy chain domain, an antibody CH2 heavy chain domain, an antibody CH3 heavy chain domain, or any combination thereof, in addition to the one or more constant region domains. An effector group may also comprise a hinge region of an antibody (such a region normally being found between the CH1 and CH2 domains of an IgG molecule). In a further embodiment of this aspect of the invention, an effector group according to the present invention is an Fc region of an IgG molecule. Advantageously, a peptide ligand- effector group according to the present invention comprises or consists of a peptide ligand Fc fusion having a tE half-life of a day or more, two days or more, 3 days or more, 4 days or more, 5 days or more, 6 days or more or 7 days or more. Most advantageously, the peptide ligand according to the present invention comprises or consists of a peptide ligand Fc fusion having a tE half-life of a day or more. Functional groups include, in general, binding groups, drugs, reactive groups for the attachment of other entities, functional groups which aid uptake of the macrocyclic peptides into cells, and the like. The ability of peptides to penetrate into cells will allow peptides against intracellular targets to be effective. Targets that can be accessed by peptides with the ability to penetrate into cells include transcription factors, intracellular signalling molecules such as tyrosine kinases and molecules involved in the apoptotic pathway. Functional groups which enable the penetration of cells include peptides or chemical groups which have been added either to the peptide or the molecular scaffold. Peptides such as those derived from such as VP22, HIV-Tat, a homeobox protein of Drosophila (Antennapedia), e.g. as described in Chen and Harrison, Biochemical Society Transactions (2007) Volume 35, part 4, p821; Gupta et al. in Advanced Drug Discovery Reviews (2004) Volume 579637. Examples of short peptides which have been shown to be efficient at translocation through plasma membranes include the 16 amino acid penetratin peptide from Drosophila Antennapedia protein (Derossi et al (1994) J Biol. &KHP^^9ROXPH^^^^^S^^^^^^^^ WKH^^^^DPLQR^DFLG^ µPRGHO^DPSKLSDWKLF^SHSWLGH¶^ ^2HKONH^et al (1998) Biochim Biophys Acts Volume 1414 p127) and arginine rich regions of the HIV TAT protein. Non peptidic approaches include the use of small molecule mimics or SMOCs that can be easily attached to biomolecules (Okuyama et al (2007) Nature Methods Volume 4 p153). Other chemical strategies to add guanidinium groups to molecules also enhance cell penetration (Elson-Scwab et al (2007) J Biol Chem Volume 282 p13585). Small molecular weight molecules such as steroids may be added to the molecular scaffold to enhance uptake into cells. One class of functional groups which may be attached to peptide ligands includes antibodies and binding fragments thereof, such as Fab, Fv or single domain fragments. In particular, antibodies which bind to proteins capable of increasing the half-life of the peptide ligand in vivo may be used. In one embodiment, a peptide ligand-effector group according to the invention has a tE half- life selected from the group consisting of: 12 hours or more, 24 hours or more, 2 days or more, 3 days or more, 4 days or more, 5 days or more, 6 days or more, 7 days or more, 8 days or more, 9 days or more, 10 days or more, 11 days or more, 12 days or more, 13 days or more, 14 days or more, 15 days or more or 20 days or more. Advantageously a peptide ligand- effector group or composition according to the invention will have a tE half-life in the range 12 to 60 hours. In a further embodiment, it will have a tE half-life of a day or more. In a further embodiment still, it will be in the range 12 to 26 hours. In one particular embodiment of the invention, the functional group is selected from a metal chelator, which is suitable for complexing metal radioisotopes of medicinal relevance. Suitable effector and / or functional groups also include chromophores and / or fluorophores. Suitable fluorophores are well known those skilled in the art and include, for example AlexaFluor compounds (such as AlexaFluor488) and Bodipy compounds (such as Bodipy558). The effector and / or functional group may also be which produces a detectable signal in the presence of a second intermediate (for example, biotin and various protein antigens). For biotin, the secondary intermediate may include streptavidin-enzyme conjugates or streptavidin-dye conjugates. Possible effector groups also include enzymes, for instance such as carboxypeptidase G2 for use in enzyme / prodrug therapy, where the peptide ligand replaces antibodies in ADEPT. In one particular embodiment of the invention, the functional group is selected from a drug, such as a cytotoxic agent for cancer therapy. Suitable examples include: alkylating agents such as cisplatin and carboplatin, as well as oxaliplatin, mechlorethamine, cyclophosphamide, chlorambucil, ifosfamide; Anti-metabolites including purine analogs azathioprine and mercaptopurine or pyrimidine analogs; plant alkaloids and terpenoids including vinca alkaloids such as Vincristine, Vinblastine, Vinorelbine and Vindesine; Podophyllotoxin and its derivatives etoposide and teniposide; Taxanes, including paclitaxel, originally known as Taxol; topoisomerase inhibitors including camptothecins: irinotecan and topotecan, and type II inhibitors including amsacrine, etoposide, etoposide phosphate, and teniposide. Further agents can include antitumour antibiotics which include the immunosuppressant dactinomycin (which is used in kidney transplantations), doxorubicin, epirubicin, bleomycin, calicheamycins, and others. In one further particular embodiment of the invention, the cytotoxic agent is selected from maytansinoids (such as DM1) or monomethyl auristatins (such as MMAE). In one embodiment, the cytotoxic agent is linked to the bicyclic peptide by a cleavable bond, such as a disulphide bond or a protease sensitive bond. In a further embodiment, the groups adjacent to the disulphide bond are modified to control the hindrance of the disulphide bond, and by this the rate of cleavage and concomitant release of cytotoxic agent. Published work established the potential for modifying the susceptibility of the disulphide bond to reduction by introducing steric hindrance on either side of the disulphide bond (Kellogg et al (2011) Bioconjugate Chemistry, 22, 717). A greater degree of steric hindrance reduces the rate of reduction by intracellular glutathione and also extracellular (systemic) reducing agents, consequentially reducing the ease by which toxin is released, both inside and outside the cell. Thus, selection of the optimum in disulphide stability in the circulation (which minimises undesirable side effects of the toxin) versus efficient release in the intracellular milieu (which maximises the therapeutic effect) can be achieved by careful selection of the degree of hindrance on either side of the disulphide bond. The hindrance on either side of the disulphide bond is modulated through introducing one or more methyl groups on either the targeting entity (here, the bicyclic peptide) or toxin side of the molecular construct. Synthesis The peptides of the present invention may be manufactured synthetically by standard techniques followed by reaction with a molecular scaffold in vitro. When this is performed, standard chemistry may be used. This enables the rapid large-scale preparation of soluble material for further downstream experiments or validation. Such methods could be accomplished using conventional chemistry such as that disclosed in Timmerman et al. (supra). Thus, the invention also relates to manufacture of polypeptides selected as set out herein, wherein the manufacture comprises optional further steps as explained below. In one embodiment, these steps are carried out on the end product polypeptide made by chemical synthesis. Peptides can also be extended, to incorporate for example another loop and therefore introduce multiple specificities. To extend the peptide, it may simply be extended chemically at its N-terminus or C-terminus or within the loops using orthogonally protected lysines (and analogues) using standard solid phase or solution phase chemistry. Standard (bio)conjugation techniques may be used to introduce an activated or activatable N- or C-terminus. Alternatively, additions may be made by fragment condensation or native chemical ligation e.g. as described in (Dawson et al.1994. Synthesis of Proteins by Native Chemical Ligation. Science 266:776-779), or by enzymes, for example using subtiligase as described in (Chang et al. Proc Natl Acad Sci U S A.1994 Dec 20; 91(26):12544-8 or in Hikari et al Bioorganic & Medicinal Chemistry Letters Volume 18, Issue 22, 15 November 2008, Pages 6000-6003). Alternatively, the peptides may be extended or modified by further conjugation through disulphide bonds. This has the additional advantage of allowing the first and second peptide to dissociate from each other once within the reducing environment of the cell. In this case, the molecular scaffold (e.g. TATA, TATB or TBMT) could be added during the chemical synthesis of the first peptide so as to react with the three cysteine groups; a further cysteine or thiol could then be appended to the N or C-terminus of the first peptide, so that this cysteine or thiol only reacted with a free cysteine or thiol of the second peptide, forming a disulfide ± linked bicyclic peptide-peptide conjugate. Similar techniques apply equally to the synthesis / coupling of two bicyclic and bispecific macrocycles, potentially creating a tetraspecific molecule. Furthermore, addition of other functional groups or effector groups may be accomplished in the same manner, using appropriate chemistry, coupling at the N- or C-termini or via side chains. In one embodiment, the coupling is conducted in such a manner that it does not block the activity of either entity. In some embodiments synthesis of a peptide ligand as provided herein may comprise solid- phase synthesis of a polypeptide as described herein. In some embodiments the solid-phase synthesis comprises Fmoc solid-phase peptide synthesis (e.g. as described in more detail herein). In some embodiments the synthesized polypeptide is cyclised with a molecular scaffold as described herein. In some embodiments the cyclised ligand is purified e.g. by lyophilisation. In some embodiments synthesis of a complex as described herein comprises reaction of a cyclised polypeptide as described herein with a linker. In some embodiments reaction of a cyclised polypeptide with a linker involves reaction of an azide group (e.g. on the linker) with an alkyne group (e.g. on the polypeptide). In some embodiments reaction of an azide group with an alkyne group takes place in the presence of a suitable azide-alkyne cycloaddition catalyst. In some embodiments a suitable catalyst comprises CuSO4. In some embodiments reaction of an azide group with an alkyne group takes place under an inert atmosphere (e.g. N2). In some embodiments reaction of a cyclised polypeptide with a linker involves reaction of an amine group (e.g. on the polypeptide) with a carboxylic acid group or activated derivative thereof (e.g. an NHS-ester group) (e.g. on the linker). In some embodiments reaction of an amine group and a carboxylic acid group or activated derivative thereof takes place in the presence of a suitable coupling agent. In some embodiments a suitable coupling agent comprises a base. Pharmaceutical Compositions According to a further aspect of the invention, there is provided a pharmaceutical composition comprising a peptide ligand or multimeric binding complex as defined herein in combination with one or more pharmaceutically acceptable excipients. Generally, the present peptide ligands will be utilised in purified form together with pharmacologically appropriate excipients or carriers. Typically, these excipients or carriers include aqueous or alcoholic / aqueous solutions, emulsions or suspensions, including saline and / or buffered media. Parenteral vehicles include sodium chloride solution, Ringer's dextrose, dextrose and sodium chloride and lactated Ringer's. Suitable physiologically- acceptable adjuvants, if necessary to keep a polypeptide complex in suspension, may be chosen from thickeners such as carboxymethylcellulose, polyvinylpyrrolidone, gelatin and alginates. Intravenous vehicles include fluid and nutrient replenishers and electrolyte replenishers, such as those based on Ringer's dextrose. Preservatives and other additives, such as antimicrobials, antioxidants, chelating agents and inert gases, may also be present (Mack (1982) Remington's Pharmaceutical Sciences, 16th Edition). The compounds of the invention can be used alone or in combination with another agent or agents. The compounds of the invention can also be used in combination with biological therapies such as nucleic acid-based therapies, antibodies, bacteriophage or phage lysins. The route of administration of pharmaceutical compositions according to the invention may be any of those commonly known to those of ordinary skill in the art. For therapy, the peptide ligands of the invention can be administered to any patient in accordance with standard techniques. Routes of administration include, but are not limited to, oral (e.g., by ingestion); buccal; sublingual; transdermal (including, e.g., by a patch, plaster, etc.); transmucosal (including, e.g., by a patch, plaster, etc.); intranasal (e.g., by nasal spray); ocular (e.g., by eyedrops); pulmonary (e.g., by inhalation or insufflation therapy using, e.g., via an aerosol, e.g., through the mouth or nose); rectal (e.g., by suppository or enema); vaginal (e.g., by pessary); parenteral, for example, by injection, including subcutaneous, intradermal, intramuscular, intravenous, intraarterial, intracardiac, intrathecal, intraspinal, intracapsular, subcapsular, intraorbital, intraperitoneal, intratracheal, subcuticular, intraarticular, subarachnoid, and intrasternal; by implant of a depot or reservoir, for example, subcutaneously or intramuscularly. Preferably, the pharmaceutical compositions according to the invention will be administered parenterally. The dosage and frequency of administration will depend on the age, sex and condition of the patient, concurrent administration of other drugs, counterindications and other parameters to be taken into account by the clinician. The peptide ligands of this invention can be lyophilised for storage and reconstituted in a suitable carrier prior to use. This technique has been shown to be effective and art-known lyophilisation and reconstitution techniques can be employed. It will be appreciated by those skilled in the art that lyophilisation and reconstitution can lead to varying degrees of activity loss and that levels may have to be adjusted upward to compensate. The compositions containing the present peptide ligands or a cocktail thereof can be administered for therapeutic treatments. In certain therapeutic applications, an adequate amount to accomplish at least partial inhibition, suppression, modulation, killing, or some other measurable parameter, of a population of selected cells is defined as a "therapeutically- effective dose". Amounts needed to achieve this dosage will depend upon the severity of the disease and the general state of the patient's own immune system, but generally range from 10 μg to 250 mg of selected peptide ligand per kilogram of body weight, with doses of between 100 μg to 25 mg / kg / dose being more commonly used. A composition containing a peptide ligand according to the present invention may be utilised in therapeutic settings to treat a microbial infection or to provide prophylaxis to a subject at risk of infection e.g. undergoing surgery, chemotherapy, artificial ventilation or other condition or planned intervention. In addition, the peptide ligands described herein may be used extracorporeally or in vitro selectively to kill, deplete or otherwise effectively remove a target cell population from a heterogeneous collection of cells. Blood from a mammal may be combined extracorporeally with the selected peptide ligands whereby the undesired cells are killed or otherwise removed from the blood for return to the mammal in accordance with standard techniques. Therapeutic Uses According to a further aspect of the invention, there is provided the peptide ligand, bicyclic peptide ligand, pharmaceutical composition, multimeric binding complex, or drug conjugate as described herein, for use in preventing, suppressing or treating a disease or disorder mediated by TLR3. According to a further aspect of the invention, there is provided a method of preventing, suppressing or treating a disease or disorder mediated by TLR3, which comprises administering to a patient in need thereof the peptide ligand, bicyclic peptide ligand, pharmaceutical composition, multimeric binding complex, or drug conjugate as described herein. According to a further aspect of the invention, there is provided the use of a peptide ligand, bicyclic peptide ligand, pharmaceutical composition, multimeric binding complex, or drug conjugate as described herein, in the manufacture of a medicament for preventing, suppressing or treating a disease or disorder mediated by TLR3. Examples of diseases or disorders mediated by TLR3 include autoimmune diseases, inflammatory conditions and cancer. According to a further aspect, there is provided a peptide ligand, bicyclic peptide ligand, pharmaceutical composition, multimeric binding complex, or drug conjugate as defined herein for use in preventing, suppressing or treating a disease or disorder selected from autoimmune diseases, inflammatory conditions, and cancer. According to a further aspect, there is provided a method of preventing, suppressing or treating a disease or disorder selected from autoimmune diseases, inflammatory conditions, and cancer, which comprises administering to a patient in need thereof the peptide ligand, bicyclic peptide ligand, pharmaceutical composition, multimeric binding complex, or drug conjugate as defined herein. According to a further aspect, there is provided use of a peptide ligand, bicyclic peptide ligand, pharmaceutical composition, multimeric binding complex, or drug conjugate as defined herein in the manufacture of a medicament for preventing, suppressing or treating a disease or disorder selected from autoimmune diseases, inflammatory conditions, and cancer. Examples of suitable autoimmune conditions include but are not limited to: rheumatoid arthritis, systemic lupus erythematosus (SLE), multiple sclerosis (MS), Type 1 diabetes, Hashimoto's thyroiditis, Graves' disease, inflammatory bowel disease (including Crohn's disease and ulcerative colitis), psoriasis, celiac disease, Sjögren's syndrome, ankylosing spondylitis, vasculitis (e.g., giant cell arteritis, Wegener's granulomatosis, polymyalgia rheumatica, myasthenia gravis, pernicious anemia, Addison's disease, autoimmune hepatitis, Goodpasture's syndrome, dermatomyositis, and sarcoidosis. Examples of suitable inflammatory conditions include but are not limited to: acne vulgaris, asthma, autoimmune diseases, autoinflammatory diseases, celiac disease, chronic prostatitis, colitis, diverticulitis, familial Mediterranean fever, glomerulonephritis, hidradenitis suppurativa, hypersensitivities, inflammatory bowel diseases, interstitial cystitis, lichen planus, mast cell activation syndrome, mastocytosis, otitis, pelvic inflammatory disease, peripheral ulcerative keratitis, pneumonia, reperfusion injury, rheumatic fever, rheumatoid arthritis, rhinitis, sarcoidosis, transplant rejection, and vasculitis. Examples of cancers (and their benign counterparts) which may be treated (or inhibited) include, but are not limited to tumours of epithelial origin (adenomas and carcinomas of various types including adenocarcinomas, squamous carcinomas, transitional cell carcinomas and other carcinomas) such as carcinomas of the bladder and urinary tract, breast, gastrointestinal tract (including the esophagus, stomach (gastric), small intestine, colon, rectum and anus), liver (hepatocellular carcinoma), gall bladder and biliary system, exocrine pancreas, kidney,lung (for example adenocarcinomas, small cell lung carcinomas, non-small cell lung carcinomas, bronchioalveolar carcinomas and mesotheliomas), head and neck (for example cancers of the tongue, buccal cavity, larynx, pharynx, nasopharynx, tonsil, salivary glands, nasal cavity and paranasal sinuses), ovary, fallopian tubes, peritoneum, vagina, vulva, penis, cervix, myometrium, endometrium, thyroid (for example thyroid follicular carcinoma), adrenal, prostate, skin and adnexae (for example melanoma, basal cell carcinoma, squamous cell carcinoma, keratoacanthoma, dysplastic naevus); haematological malignancies (i.e. leukemias, lymphomas) and premalignant haematological disorders and disorders of borderline malignancy including haematological malignancies and related conditions of lymphoid lineage (for example acute lymphocytic leukemia [ALL], chronic lymphocytic leukemia [CLL], B-cell lymphomas such as diffuse large B-cell lymphoma [DLBCL], follicular O\PSKRPD^^%XUNLWW¶V^ lymphoma, mantle cell lymphoma, T-cell lymphomas and leukaemias, QDWXUDO^NLOOHU^ >1.@^FHOO^ O\PSKRPDV^^+RGJNLQ¶V^ O\PSKRPDV^^KDLU\^FHOO^ OHXNDHPLD^^PRQRFORQDO^ gammopathy of uncertain significance, plasmacytoma, multiple myeloma, and post-transplant lymphoproliferative disorders), and haematological malignancies and related conditions of myeloid lineage (for example acute myelogenousleukemia [AML], chronic myelogenousleukemia [CML], chronic myelomonocyticleukemia [CMML], hypereosinophilic syndrome, myeloproliferative disorders such as polycythaemia vera, essential thrombocythaemia and primary myelofibrosis, myeloproliferative syndrome, myelodysplastic syndrome, and promyelocyticleukemia); tumours of mesenchymal origin, for example sarcomas of soft tissue, bone or cartilage such as osteosarcomas, fibrosarcomas, chondrosarcomas, rhabdomyosarcomas,leiomyosarcomas, liposarcomas, angiosarcomas, .DSRVL¶V^ VDUFRPD^^ (ZLQJ¶V^ VDUFRPD^^ V\QRYLDO^ VDUFRPDV^^ HSLWKHOLRLG^ VDUFRPDV^^ gastrointestinal stromal tumours, benign and malignant histiocytomas, and dermatofibrosarcomaprotuberans; tumours of the central or peripheral nervous system (for example astrocytomas, gliomas and glioblastomas, meningiomas, ependymomas, pineal tumours and schwannomas); endocrine tumours (for example pituitary tumours, adrenal tumours, islet cell tumours, parathyroid tumours, carcinoid tumours and medullary carcinoma of the thyroid); ocular and adnexal tumours (for example retinoblastoma); germ cell and trophoblastic tumours (for example teratomas, seminomas, dysgerminomas, hydatidiform moles and choriocarcinomas); and paediatric and embryonal tumours (for example medulloblastoma, neuroblastoma, Wilms tumour, and primitive neuroectodermal tumours); or syndromes, congenital or otherwise, which leave the patient susceptible to malignancy (for example Xeroderma Pigmentosum). References herein to the term "prevention" involves administration of the protective composition prior to the induction of the disease. "Suppression" refers to administration of the composition after an inductive event, but prior to the clinical appearance of the disease. "Treatment" involves administration of the protective composition after disease symptoms become manifest. Animal model systems which can be used to screen the effectiveness of the peptide ligands in protecting against or treating the disease are available. The use of animal model systems is facilitated by the present invention, which allows the development of polypeptide ligands which can cross react with human and animal targets, to allow the use of animal models. The invention is further described below with reference to the following examples. EXAMPLES Materials and Methods Bicyclic peptides were synthesized on Rink amide resin using standard Fmoc (9- fluorenylmethyloxycarbonyl) solid-phase peptide synthesis, either by manual coupling (for large scale) or using a Biotage SyroII automated peptide synthesizer (for small scale). Following TFA-based cleavage from the resin, peptides were precipitated with diethyl ether and dissolved in 50:50 acetonitrile / water. The crude peptides (at ^1 mM concentration) were then cyclized with 1.3 equiv. of the scaffold, using ammonium bicarbonate (100 mM) as a base. Completion of cyclization was determined by matrix-assisted laser desorption ionization time-of-flight (MALDI-72)^^RU^ / &í06^^2QFH^FRPSOHWH^^WKH^F\FOL]DWLRQ^UHDFWLRQ^ZDV^TXHQFKHG^ using N-acetyl cysteine (10 equiv. with respect to the peptide), and the solutions were lyophilized. The residue was dissolved in an appropriate solvent and purified by RP-HPLC. Peptide fractions of sufficient purity and the correct molecular weight (verified by either MALDI- 72)^DQG^+3 / &^RU^ / &í06^^ZHUH^SRROHG^DQG^O\RSKLOL]HG^^&RQcentrations were determined by UV absorption using the extinction coefficient at 280 nm, which was based on extinction coefficients of aromatic amino acids at 280nM. For example, Trp and Tyr as well non-natural amino acids such as 5FTrp, etc. All amino acids, unless noted otherwise, were used in the L-configurations. References herein WR^DPLQR^DFLGV^ZLWK^D^³G´^SUHIL[^^L^H^^G&^RU^G$^^UHIHU^WR^DPLQR^DFLGV^LQ^WKH^'-configurations. Preparation of Multimeric Binding Complexes Example 1: Procedure for preparation of BCY15926 A mixture of compound 1 (20.0 mg, 4.21 μmol, 1.0 eq.), compound 2 (42.6 mg, 18.5 μmol, 4.4 eq.), and THPTA (7.30 mg, 16.8 μmol, 4.0 eq.) was dissolved in t-BuOH / H2O (1:1, 1.0 mL, pre-degassed by purging with N2for 3 times), and then an aqueous solution of CuSO4(0.4 M, 21.0 μL, 2.0 eq.) and VcNa (3.30 mg, 16.8 μmol, 4.0 eq.) were added under N2. The pH of this solution was adjusted to 8 by dropwise addition of 0.2 M NH4HCO3(in 1:1 t-BuOH / H2O), and the solution turned to be light yellow. The reaction was stirred at 25-30 °C for 1 hr under N2atmosphere. LC-MS showed compound 1 was consumed completely, and one main peak with desired m / z (calculated MW: 13904, observed m / z: 1391.3 ([M+10H]10+)) was detected. The reaction mixture was filtered to remove the undissolved residue. The crude was purified by prep-HPLC (TFA condition), and BCY15926 (13.2 mg, 9.27 μmol, 29.3% yield, 97.6% purity) was obtained as a white solid. A mixture of compound 4 (15.0 mg, 23.8 μmol, 1.0 eq.), compound 5 (39.7 mg, 33.3 μmol, 1.4 eq.) and DIEA (12.4 μL, 71.3 μmol, 4.0 eq.) was dissolved in DMF (0.5 mL). The reaction was stirred at 25-30 °C for 1 hr. LC-MS showed compound 4 was consumed completely and one main peak with desired m / z (MW: 1708.85, observed m / z: 854.9([M+2H]2+)) was detected. The reaction mixture was filtered to remove the undissolved residue. The crude was then purified by prep-HPLC (TFA condition). Compound 6 (18.0 mg, 10.0 μmol, 42.2% yield, 95.3% purity) was obtained as an orange solid. A mixture of compound 6 (3.00 mg, 1.76 μmol, 1.0 eq.), BCY15751 (8.80 mg, 3.86 μmol, 2.2 eq.), and THPTA (1.60 mg, 3.69 μmol, 2.1 eq.) was dissolved in t-BuOH / H2O (1:1, 0.2 mL, pre-degassed by purging with N2for 3 times), and then an aqueous solution of CuSO4(0.4 M, .8.80 μL, 2.0 eq.) and VcNa (1.40 mg, 3.51 μmol, 4.0 eq.) were added under N2. The pH of this solution was adjusted to 8 by dropwise addition of 0.2 M NH4HCO3(in 1:1 t-BuOH / H2O), and the solution turned to be yellow green. The reaction was stirred at 25-30 °C for 1 hr under N2atmosphere. LC-MS showed compound 6 was consumed completely, and one main peak with desired m / z (calculated MW: 6286.09, observed m / z: 1257.9 ([M+5H]5+), 1048.6 ([M+6H]6+)) was detected. The reaction mixture was filtered to remove the undissolved residue. The crude was purified by prep-HPLC (TFA condition), and BCY16282 (3.40 mg, 0.54 μmol, 28.7% yield, 93.2% purity) was obtained as an orange solid. Example 3: Procedure for preparation of BCY25831 A mixture of compound 1 (5.0 mg, 2.03 μmol, 1.0 eq.), compound 2 (22.1 mg, 9.15 μmol, 4.5 eq.), and THPTA (3.50 mg, 8.13 μmol, 4.0 eq.) was dissolved in t-BuOH / H2O (1:1, 0.2 mL, pre-degassed by purging with N2for 3 times), and then an aqueous solution of CuSO4(0.4 M, 20.3 μL,4.0 eq.) and VcNa (3.20 mg, 16.3 μmol, 8.0 eq.) were added under N2. The pH of this solution was adjusted to 8 by dropwise addition of 0.2 M NH4HCO3(in 1:1 t-BuOH / H2O), and the solution turned to be light yellow. The reaction was stirred at 0 °C for 0.5 hr under N2atmosphere. LC-MS showed compound 1 was consumed completely, and one main peak with desired m / z (calculated MW: 12137.87, observed m / z: 1349.4([M+9H]9+) was detected. The mixture was filtered to remove the undissolved residue. The crude was purified by prep-HPLC (TFA condition) to afford BCY25831 (5.70 mg, 0.45 μmol, 22.3% yield, 96.3% purity) as a white solid. Example 4: Procedure for preparation of BCY25832 A mixture of compound 1 (5.0 mg, 2.64 μmol, 1.0 eq.), compound 2 (21.1 mg, 8.72 μmol, 3.3 eq.), and THPTA (3.50 mg, 7.93 μmol, 3.0 eq.) was dissolved in t-BuOH / H2O (1:1, 0.2 mL, pre-degassed by purging with N2for 3 times), and then an aqueous solution of CuSO4(0.4 M, 19.8 μL,3.0 eq.) and VcNa (3.10 mg, 15.9 μmol, 6.0 eq.) were added under N2. The pH of this solution was adjusted to 8 by dropwise addition of 0.2 M NH4HCO3(in 1:1 t-BuOH / H2O), and the solution turned to be light yellow. The reaction was stirred at 0 °C for 0.5 hr under N2atmosphere. LC-MS showed compound 1 was consumed completely, and one main peak with desired m / z (calculated MW: 9150.48, observed m / z: 1307.2([M+7H]7+) was detected. The mixture was filtered to remove the undissolved residue. The crude was purified by prep-HPLC (TFA condition) to afford BCY25832 (7.50 mg, 0.80 μmol, 30.3% yield, 97.9% purity) as a white solid. Example 5: Procedure for preparation of BCY26427 A mixture of compound 1 (6.0 mg, 5.22 μmol, 1.0 eq.), compound 2 (27.7 mg, 11.5 μmol, 2.2 eq.), and THPTA (4.5 mg, 10.4 μmol, 2.0 eq.) was dissolved in t-BuOH / H2O (1:1, 0.3 mL, pre- degassed by purging with N2for 3 times), and then an aqueous solution of CuSO4(0.4 M, 26.1 μL,2.0 eq.) and VcNa (4.1 mg, 20.88 μmol, 4.0 eq.) were added under N2. The pH of this solution was adjusted to 8 by dropwise addition of 0.2 M NH4HCO3(in 1:1 t-BuOH / H2O), and the solution turned to be dark blue. The reaction was stirred at 0 °C for 0.5 hr under N2atmosphere. LC-MS showed compound 1 was consumed completely, and one main peak with desired m / z (calculated MW: 5988.8, observed m / z: 1198.5 ([M+5H]5+) was detected. The mixture was filtered to remove the undissolved residue. The crude was purified by prep-HPLC (TFA condition), and BCY26427 (13.8 mg, 2.26 μmol, 43.4% yield, 98.2% purity) was obtained as a white solid. Example 6: Procedure for preparation of BCY26435 A mixture of compound 1 (10.0 mg, 8.70 μmol, 1.0 eq.), compound 2 (43.5 mg, 19.1 μmol, 2.2 eq.), and THPTA (7.56 mg, 17.4 μmol, 2.0 eq.) was dissolved in t-BuOH / H2O (1:1, 0.6 mL, pre-degassed by purging with N2 for 3 times), and then an aqueous solution of CuSO4 (0.4 M, 43.5 μL,2.0 eq.) and VcNa (6.89 mg, 34.8 μmol, 4.0 eq.) were added under N2. The pH of this solution was adjusted to 8 by dropwise addition of 0.2 M NH4HCO3(in 1:1 t-BuOH / H2O), and the solution turned to be dark blue. The reaction was stirred at 25 °C for 0.5 hr under N2atmosphere. LC-MS showed compound 1 was consumed completely, and one main peak with desired m / z (calculated MW: 5694.57, observed m / z: 949.9 ([M+6H]6+) was detected. The mixture was filtered to remove the undissolved residue. The crude was purified by prep-HPLC (TFA condition), and BCY26435 (20.2 mg, 3.41 μmol, 39.2% yield, 96.2% purity) was obtained as a white solid. Example 7: Procedure for preparation of BCY26437 A mixture of compound 1 (11.0 mg, 5.82 μmol, 1.0 eq.), compound 2 (43.6 mg, 19.2 μmol, 3.3 eq.), and THPTA (7.58 mg, 17.5 μmol, 3.0 eq.) was dissolved in t-BuOH / H2O (1:1, 0.6 mL, pre-degassed by purging with N2for 3 times), and then an aqueous solution of CuSO4(0.4 M, 43.6 μL,3.0 eq.) and VcNa (6.91 mg, 34.9 μmol, 6.0 eq.) were added under N2. The pH of this solution was adjusted to 8 by dropwise addition of 0.2 M NH4HCO3(in 1:1 t-BuOH / H2O), and the solution turned to be dark blue. The reaction was stirred at 25 °C for 0.5 hr under N2atmosphere. LC-MS showed compound 1 was consumed completely, and one main peak with desired m / z (calculated MW: 8709.05, observed m / z: 1244.9 ([M+7H]7+) was detected. The mixture was filtered to remove the undissolved residue. The crude was purified by prep-HPLC (TFA condition), and BCY26437 (19.0 mg, 2.06 μmol, 35.5% yield, 94.6% purity) was obtained as a white solid. Example 8: Procedure for preparation of BCY26438 A mixture of compound 1 (5.00 mg, 3.17 μmol, 1.0 eq.), compound 2 (32.4 mg, 14.3 μmol, 4.5 eq.), and THPTA (5.50 mg, 12.7 μmol, 4.0 eq.) was dissolved in t-BuOH / H2O (1:1, 0.4 mL, pre-degassed by purging with N2for 3 times), and then an aqueous solution of CuSO4(0.4 M, 31.7 μL, 4.0 eq.) and VcNa (5.00 mg, 25.4 μmol, 8.0 eq.) were added under N2. The pH of this solution was adjusted to 8 by dropwise addition of 0.2 M NH4HCO3(in 1:1 t-BuOH / H2O), and the solution turned to be dark blue. The reaction was stirred at 0 °C for 0.5 hr under N2atmosphere. LC-MS showed compound 1 was consumed completely, and one main peak with desired m / z (calculated MW: 10668.3, observed m / z: 1334.4 ([M+8H]8+) was detected. The mixture was filtered to remove the undissolved residue. The crude was purified by prep-HPLC (TFA condition), and BCY26438 (3.40 mg, 0.29 μmol, 9.1% yield, 90.2% purity) was obtained as a white solid. Example 9: Procedure for preparation of BCY26439 A mixture of compound 1 (5.0 mg, 2.03 μmol, 1.0 eq.), compound 2 (20.8 mg, 9.15 μmol, 4.5 eq.), and THPTA (3.50 mg, 8.13 μmol, 4.0 eq.) was dissolved in t-BuOH / H2O (1:1, 0.2 mL, pre-degassed by purging with N2for 3 times), and then an aqueous solution of CuSO4(0.4 M, 20.3 μL,4.0 eq.) and VcNa (3.20 mg, 16.3 μmol, 8.0 eq.) were added under N2. The pH of this solution was adjusted to 8 by dropwise addition of 0.2 M NH4HCO3(in 1:1 t-BuOH / H2O), and the solution turned to be light yellow. The reaction was stirred at 0 °C for 0.5 hr under N2atmosphere. LC-MS showed compound 1 was consumed completely, and one main peak with desired m / z (calculated MW: 11549.45, observed m / z: 1444.4([M+8H]8+) was detected. The mixture was filtered to remove the undissolved residue. The crude was purified by prep-HPLC (TFA condition) to afford BCY26439 (4.0 mg, 0.30 μmol, 15.8% yield, 92.8% purity) as a white solid. Example 10: Procedure for preparation of BCY28218 (Biotinylated dimer) A mixture of compound 1 (6.00 mg, 3.53 μmol, 1.0 eq.), compound 2 (17.6 mg, 7.76 μmol, 2.2 eq.), and THPTA (3.06 mg, 7.05 μmol, 2.0 eq.) was dissolved in t-BuOH / H2O (1:1, 0.3 mL, pre-degassed by purging with N2for 3 times), and then an aqueous solution of CuSO4(0.4 M, 17.6 μL, 2.0 eq.) and VcNa (2.79 mg, 14.1 μmol, 4.0 eq.) were added under N2. The reaction was stirred at 0 °C for 0.5 hr under N2atmosphere. LC-MS showed compound 1 was consumed completely and one main peak with desired m / z (calculated MW: 6247.29 observed m / z: 1042.0 ([M+6H]6+)) was detected. The mixture was filtered to remove the undissolved residue. The crude product was purified by prep-HPLC (TFA condition), and BCY28218 (8.50 mg, 1.35 μmol, 38.2% yield, 98.9% purity) was obtained as a white solid. Example 11: Procedure for preparation of BCY28224 (Biotinylated dimer) A mixture of compound 1 (6.00 mg, 3.44 μmol, 1.0 eq.), compound 2 (22.1 mg, 7.56 μmol, 2.2 eq.), and THPTA (2.99 mg, 6.87 μmol, 2.0 eq.) was dissolved in t-BuOH / H2O (1:1, 0.3 mL, pre-degassed by purging with N2for 3 times), and then an aqueous solution of CuSO4(0.4 M, 17.2 μL, 2.0 eq.) and VcNa (2.72 mg, 13.7 μmol, 4.0 eq.) were added under N2. The reaction was stirred at 0 °C for 0.5 hr under N2atmosphere. LC-MS showed compound 1 was consumed completely and one main peak with desired m / z (calculated MW: 7604.74 observed m / z: 1087.3 ([M+7H]7+)) was detected. The mixture was filtered to remove the undissolved residue. The crude was purified by prep-HPLC (TFA condition), and BCY28224 (7.20 mg, 0.907 μmol, 26.4% yield, 95.8% purity) was obtained as a white solid. Biological Data SPR Binding TLR3 monomer SPR: surface plasma resonance (SPR) was performed on a Biacore T200 or 8K+ to determine the ka^0í^^Ví^^^^Nd^Ví^^^^DQG^.D(M) values of peptides binding to TLR3 target protein. Recombinant human TLR3-Avi[bt]-Fc-Flag-his protein was custom produced at Charles River laboratories in Hi5 insect cells. The protein was captured on CM5 chips (GE Healthcare) using goat-anti-human IgG at surface density ranging between ~1100-1800 RU. Standard SPR screening experiments were run in acidic running buffer 25mM MES , 100mM NaCl, 0.05% Tween 20 at pH5.5 since dsRNA binding to TLR3 is known to be pH-sensitive (Leonard et al (2008) PNAS 105(1), 258-265). In some experiments binding was also confirmed at neutral pH range using pH 7.425mM HEPES, 100mM NaCl, 0.05% Tween 20 buffer. An 8-fold dilution series of the peptides with maximum tested concentration 30 mM peptide were prepared in the running buffer with a final dimethyl sulfoxide (DMSO) concentration of 0.5%. Data were corrected for DMSO excluded volume effects. The peptides ZHUH^LQMHFWHG^RYHU^WKH^FKLS^DW^^^^^&^DW^D^IORZ^UDWH^RI^^^^^ / ^PLQ^^$OO^GDWD^ZHUH^GRXEOH^UHIHUHQFHG^ for blank injections and reference surfaces using standard processing procedures. Data was fitted to a 1:1 binding model with either steady-state or kinetics where appropriate (in Biacore evaluation software). Acknowledgements Charles River laboratories (Harlow and Chesterford park) for performing SPR analysis. Selected monomeric bicyclic peptides of the invention were tested in the above mentioned SPR binding assay and the results are shown in Table 4A: Table 4A BCY Number KD(M) BCY19585 9.00 x 10-7BCY19586 7.10 x 10-7BCY23135 3.32 x 10-6BCY23136 3.60 x 10-6BCY15810 3.45 x 10-6BCY20791 2.85 x 10-6BCY16655 9.55 x 10-6BCY16656 5.53 x 10-6BCY16657 3.09 x 10-6BCY16658 7.80 x 10-6BCY16659 8.76 x 10-6BCY16660 2.18 x 10-5 BCY16661 1.60 x 10-6BCY15207 1.51 x 10-6BCY15750 2.04 x 10-6BCY15811 2.33 x 10-6BCY15812 9.04 x 10-7BCY15813 1.36 x 10-6BCY15814 7.31 x 10-7BCY17031 7.77 x 10-7BCY17032 3.21 x 10-7BCY17033 9.69 x 10-7BCY17038 6.91 x 10-7 BCY17041 2.29 x 10-7BCY17042 1.42 x 10-6BCY19197 4.29 x 10-7BCY19384 1.90 x 10-6BCY19582 9.62 x 10-7BCY16639 3.61 x 10-8BCY16663 2.51 x 10-7BCY16664 5.37 x 10-7BCY16665 2.79 x 10-6BCY16666 1.24 x 10-6BCY16667 3.84 x 10-7BCY17238 3.81 x 10-7BCY19192 5.25 x 10-7BCY19193 1.69 x 10-6BCY19194 4.07 x 10-7BCY19195 8.24 x 10-7BCY19196 4.30 x 10-7BCY19198 8.53 x 10-7BCY19199 1.26 x 10-6BCY19200 1.01 x 10-6BCY19203 7.00 x 10-6BCY19205 1.28 x 10-6BCY19206 6.40 x 10-7BCY21608 9.62 x 10-7BCY15727 6.76 x 10-6BCY17452 4.94 x 10-6BCY19157 6.78 x 10-6BCY19158 1.17 x 10-5 BCY19159 9.40 x 10-6BCY19161 9.20 x 10-6BCY19162 1.61 x 10-6BCY19163 5.90 x 10-6BCY19164 4.89 x 10-6BCY19165 1.49 x 10-5 BCY19166 6.00 x 10-6 BCY19167 1.50 x 10-5 BCY19170 2.65 x 10-5 BCY19171 6.42 x 10-6BCY19177 9.52 x 10-7BCY19179 1.44 x 10-5 BCY19181 1.71 x 10-5 BCY19184 9.20 x 10-6BCY19185 1.85 x 10-5 BCY19187 4.70 x 10-6BCY19188 1.16 x 10-5 BCY19189 5.66 x 10-6BCY19284 1.08 x 10-5 BCY19385 3.30 x 10-6BCY19580 5.71 x 10-6BCY19995 2.56 x 10-5 BCY21040 4.89 x 10-7BCY21192 5.11 x 10-6BCY21193 8.90 x 10-6BCY21194 8.60 x 10-6BCY21195 7.24 x 10-6BCY21196 1.25 x 10-5 BCY21197 1.09 x 10-6BCY21198 4.65 x 10-6BCY21199 9.25 x 10-7BCY21200 4.69 x 10-6BCY21201 5.42 x 10-6BCY21631 1.84 x 10-6BCY21632 1.75 x 10-6BCY21633 1.90 x 10-6BCY21634 2.85 x 10-6BCY21635 2.98 x 10-6BCY21636 3.57 x 10-6BCY21637 2.39 x 10-6BCY21993 8.90 x 10-7BCY21994 1.03 x 10-6 BCY21995 1.70 x 10-7BCY21996 1.54 x 10-7BCY21997 1.27 x 10-7BCY21998 1.62 x 10-7BCY22499 6.85 x 10-7BCY23137 2.55 x 10-6BCY23174 4.07 x 10-6BCY23179 2.74 x 10-6BCY23702 4.82 x 10-7BCY23703 8.18 x 10-7BCY23704 7.41 x 10-7BCY23705 9.91 x 10-7BCY23706 1.33 x 10-7BCY23707 1.03 x 10-6BCY25601 7.75 x 10-7BCY25602 1.19 x 10-6BCY15729 4.48 x 10-6BCY15210 2.36 x 10-6BCY15752 2.57 x 10-6BCY15731 8.90 x 10-7BCY15733 1.35 x 10-6BCY15735 5.23 x 10-7BCY15211 3.36 x 10-6BCY15737 1.75 x 10-6BCY15739 8.33 x 10-7BCY17047 9.40 x 10-7BCY17049 9.00 x 10-7BCY17051 1.24 x 10-6BCY17055 2.14 x 10-7BCY17057 1.22 x 10-6BCY17058 9.09 x 10-8BCY17059 6.10 x 10-7BCY17061 4.22 x 10-7BCY19386 1.28 x 10-6BCY19581 1.77 x 10-6 BCY15741 8.50 x 10-7BCY15743 1.59 x 10-6BCY15745 3.79 x 10-7BCY16668 9.59 x 10-7BCY16669 1.86 x 10-7BCY16670 1.42 x 10-7BCY16671 2.63 x 10-7BCY18510 2.77 x 10-6BCY18511 2.49 x 10-8BCY18514 5.59 x 10-7BCY18515 2.65 x 10-7BCY18518 6.80 x 10-6BCY18519 2.45 x 10-7BCY18520 1.05 x 10-6BCY25826 1.48 x 10-8BCY16672 1.38 x 10-6BCY16673 2.25 x 10-7BCY17237 2.03 x 10-7BCY16674 1.29 x 10-6BCY15200 1.65 x 10-6BCY15747 2.69 x 10-6BCY17071 3.70 x 10-6BCY17081 1.98 x 10-6BCY19281 8.30 x 10-6BCY16997 3.14 x 10-6BCY18125 2.00 x 10-6BCY19741 1.89 x 10-6BCY21538 3.57 x 10-6BCY21539 4.55 x 10-6BCY21540 2.19 x 10-6BCY21541 4.37 x 10-6BCY21542 2.54 x 10-6BCY21543 3.32 x 10-6BCY21544 6.39 x 10-6BCY21550 3.49 x 10-6 BCY21551 1.54 x 10-6BCY21558 2.56 x 10-6BCY21561 6.44 x 10-6BCY21562 4.65 x 10-6BCY21564 4.01 x 10-6BCY21565 6.28 x 10-6BCY21566 1.80 x 10-6BCY21567 1.60 x 10-6BCY21568 6.06 x 10-6BCY21569 5.01 x 10-6BCY21769 1.73 x 10-6BCY21775 1.36 x 10-6BCY21777 3.50 x 10-6BCY16998 1.80 x 10-6BCY16999 1.23 x 10-6BCY19387 6.70 x 10-6BCY18126 1.12 x 10-6BCY20723 7.27 x 10-6BCY20725 1.88 x 10-6BCY20731 7.39 x 10-6BCY20732 1.82 x 10-6BCY20734 1.15 x 10-6BCY20735 1.77 x 10-6BCY20736 9.71 x 10-7BCY20737 2.28 x 10-6BCY20738 2.28 x 10-6BCY20741 9.13 x 10-7BCY20742 1.45 x 10-6BCY20743 2.30 x 10-6BCY20746 1.40 x 10-6BCY20747 3.99 x 10-6BCY20748 2.60 x 10-6BCY20749 9.62 x 10-7BCY20751 3.00 x 10-5 BCY20752 3.59 x 10-6 BCY20756 4.15 x 10-6BCY20757 1.74 x 10-6BCY20758 7.95 x 10-6BCY20759 9.70 x 10-6BCY20760 1.71 x 10-6BCY20761 2.02 x 10-6BCY20762 3.05 x 10-6BCY20763 1.89 x 10-6BCY20764 1.25 x 10-6BCY20765 4.58 x 10-6BCY20766 7.75 x 10-6BCY21770 4.88 x 10-7BCY21771 1.58 x 10-7BCY21772 3.43 x 10-7BCY21774 4.80 x 10-7BCY21778 1.72 x 10-7BCY23767 8.27 x 10-8BCY18127 1.73 x 10-6BCY19742 1.00 x 10-6BCY17001 7.96 x 10-6BCY18128 2.72 x 10-6BCY19743 1.64 x 10-6BCY18129 2.27 x 10-6BCY19744 1.89 x 10-6BCY24131 4.56 x 10-6BCY24135 4.02 x 10-6BCY24442 8.03 x 10-5 BCY24443 7.78 x 10-6BCY24444 7.98 x 10-6BCY24445 6.89 x 10-6BCY24450 3.51 x 10-6BCY24451 3.28 x 10-6BCY24452 5.20 x 10-6BCY24453 3.89 x 10-6BCY24456 2.78 x 10-6 BCY24457 3.41 x 10-6BCY24458 4.54 x 10-6BCY24459 1.48 x 10-6BCY24462 5.42 x 10-6BCY24466 4.33 x 10-6BCY24467 3.59 x 10-6BCY24468 9.62 x 10-6BCY24469 6.65 x 10-6BCY24471 7.18 x 10-6BCY24472 4.00 x 10-6BCY24473 2.12 x 10-6BCY24474 5.98 x 10-6BCY24475 6.24 x 10-6BCY24477 2.69 x 10-6BCY24478 6.23 x 10-6BCY24479 5.81 x 10-6BCY24480 3.79 x 10-6BCY24481 3.90 x 10-6BCY24482 6.52 x 10-6BCY24483 2.74 x 10-6BCY24484 4.41 x 10-6BCY24485 7.88 x 10-6BCY24486 1.18 x 10-6BCY24487 4.51 x 10-6BCY24488 3.55 x 10-6BCY24489 2.03 x 10-6BCY24490 8.29 x 10-6BCY24491 2.61 x 10-6BCY24492 4.31 x 10-6BCY24493 9.67 x 10-6BCY24495 5.61 x 10-6BCY24496 3.80 x 10-6BCY24497 4.24 x 10-6BCY24498 4.96 x 10-6BCY24499 3.08 x 10-6 BCY24500 3.51 x 10-6BCY24501 4.62 x 10-6BCY24503 3.98 x 10-6BCY24504 4.92 x 10-6BCY24505 3.54 x 10-6BCY24506 8.46 x 10-6BCY24509 4.32 x 10-6BCY25863 2.37 x 10-6BCY25865 1.99 x 10-6BCY25866 1.01 x 10-6BCY28838 2.34 x 10-7BCY28839 2.92 x 10-7BCY25861 1.21 x 10-6BCY28843 1.58 x 10-6BCY28844 7.72 x 10-7BCY25859 8.24 x 10-7BCY17002 2.20 x 10-6BCY19745 1.26 x 10-6BCY18130 1.87 x 10-7BCY20847 1.24 x 10-7BCY20848 8.42 x 10-7BCY20849 8.46 x 10-7BCY20850 7.87 x 10-7BCY20851 4.60 x 10-7BCY20852 3.68 x 10-7BCY20853 3.72 x 10-7BCY21607 1.14 x 10-8BCY21615 1.03 x 10-7BCY21616 2.19 x 10-7BCY21617 5.02 x 10-8BCY21618 5.16 x 10-7BCY21619 7.60 x 10-7BCY21620 2.46 x 10-7BCY21622 2.54 x 10-8BCY21623 1.48 x 10-7 BCY21624 7.30 x 10-7BCY21625 2.37 x 10-7BCY21626 1.51 x 10-6BCY21627 5.43 x 10-7BCY22879 2.61 x 10-7BCY22880 3.74 x 10-7BCY23043 9.46 x 10-8BCY23044 1.55 x 10-7BCY23045 1.34 x 10-7BCY23046 1.44 x 10-7BCY23047 1.19 x 10-7BCY23050 2.60 x 10-7BCY23051 6.15 x 10-8BCY23052 2.64 x 10-7BCY23053 2.55 x 10-7BCY23054 1.06 x 10-6BCY23058 2.13 x 10-7BCY23059 1.09 x 10-6BCY23062 1.32 x 10-7BCY23063 2.55 x 10-7BCY23064 4.93 x 10-7BCY23066 2.53 x 10-7BCY23067 1.29 x 10-7BCY23068 1.69 x 10-8BCY23071 1.26 x 10-6BCY23072 3.87 x 10-7BCY23073 3.56 x 10-7BCY23074 2.64 x 10-7BCY23075 7.81 x 10-8BCY23079 2.81 x 10-7BCY23080 8.06 x 10-8BCY23081 1.51 x 10-7BCY27058 2.96 x 10-8BCY27059 1.13 x 10-8BCY27060 1.02 x 10-8 BCY27061 2.30 x 10-8BCY27062 1.75 x 10-8BCY27063 4.00 x 10-8BCY27064 1.59 x 10-8BCY27065 1.32 x 10-8BCY27066 1.75 x 10-8BCY27067 4.50 x 10-7BCY27068 1.57 x 10-7BCY18131 2.90 x 10-7BCY18132 2.58 x 10-7BCY17006 9.00 x 10-7BCY18134 3.11 x 10-6BCY19746 1.66 x 10-6BCY17007 1.52 x 10-6BCY18135 7.75 x 10-7BCY18136 5.00 x 10-7BCY19747 9.13 x 10-7BCY17012 7.70 x 10-7BCY18251 1.11 x 10-6BCY19587 1.04 x 10-6BCY21485 1.83 x 10-6BCY21490 1.58 x 10-6BCY21493 1.12 x 10-6BCY21495 1.63 x 10-6BCY21497 1.33 x 10-6BCY21498 9.23 x 10-6BCY21500 5.80 x 10-6BCY21502 5.18 x 10-6BCY21503 1.29 x 10-6BCY21504 6.88 x 10-7BCY21505 5.19 x 10-6BCY21506 2.23 x 10-6BCY21507 7.72 x 10-6BCY21508 2.76 x 10-6BCY21510 6.29 x 10-6 BCY21515 1.75 x 10-6BCY21517 1.68 x 10-6BCY21518 1.99 x 10-6BCY21519 1.36 x 10-6BCY21521 8.10 x 10-6BCY21522 7.55 x 10-6BCY21523 9.88 x 10-6BCY21527 8.16 x 10-7BCY21528 2.68 x 10-6BCY21773 1.56 x 10-5 BCY21776 2.72 x 10-6BCY19930 7.28 x 10-7BCY19931 8.81 x 10-7BCY19932 5.94 x 10-7BCY18253 2.41 x 10-6BCY19588 3.87 x 10-6BCY19933 6.06 x 10-6BCY19934 1.15 x 10-6BCY19935 6.73 x 10-6BCY19936 3.23 x 10-7BCY21606 1.93 x 10-7BCY23138 2.51 x 10-7BCY23139 7.39 x 10-7BCY23140 1.20 x 10-6BCY23141 4.82 x 10-6BCY24613 3.25 x 10-7BCY32061 1.27 x 10-6BCY32062 2.36 x 10-7BCY32065 1.10 x 10-6BCY32066 1.99 x 10-7BCY32069 2.20 x 10-7BCY32071 1.55 x 10-7BCY32072 6.24 x 10-7BCY32074 2.82 x 10-7BCY32075 1.31 x 10-6 BCY32076 1.21 x 10-5 BCY32077 2.16 x 10-6BCY32078 3.35 x 10-6BCY32079 6.66 x 10-7BCY32080 8.46 x 10-7BCY32081 3.99 x 10-7BCY32082 1.19 x 10-5 BCY32083 6.60 x 10-7BCY32084 8.94 x 10-7BCY32085 1.48 x 10-5 BCY32086 1.66 x 10-7BCY32087 2.06 x 10-5 BCY32088 5.49 x 10-7BCY32089 1.54 x 10-6BCY32090 1.09 x 10-6BCY32091 4.54 x 10-7BCY32092 7.44 x 10-7BCY32093 1.09 x 10-6BCY32095 1.01 x 10-6BCY32096 3.26 x 10-5 BCY32098 7.36 x 10-7BCY32099 2.40 x 10-7BCY32100 2.55 x 10-7BCY32101 4.25 x 10-6BCY32103 1.65 x 10-5 BCY32104 4.46 x 10-6BCY32105 1.16 x 10-6BCY32106 7.43 x 10-7BCY32107 9.57 x 10-5 BCY32108 3.85 x 10-5 BCY32109 4.52 x 10-6BCY32110 4.56 x 10-5 BCY32112 5.42 x 10-6BCY32113 1.50 x 10-6BCY32114 6.22 x 10-7 BCY32115 4.27 x 10-7BCY32116 9.89 x 10-7BCY32117 1.69 x 10-6BCY32120 1.33 x 10-6BCY32121 1.67 x 10-7BCY32122 4.35 x 10-7BCY32123 3.16 x 10-7BCY32124 7.14 x 10-7BCY32125 2.41 x 10-5 BCY32126 5.26 x 10-7BCY32127 4.24 x 10-7BCY32128 5.83 x 10-7BCY19937 4.08 x 10-6BCY19938 1.74 x 10-6BCY19939 2.45 x 10-6BCY19940 9.11 x 10-7BCY19941 3.53 x 10-6BCY19942 7.57 x 10-6BCY19943 2.43 x 10-6Selected multimeric binding complexes of the invention were tested in the above mentioned SPR binding assay and the results are shown in Table 4B: Table 4B BCY number KD (M) BCY21481 9.61 x 10-7BCY21483 1.58 x 10-6BCY28229 4.94 x 10-8BCY28230 6.91 x 10-8BCY29425 3.46 x 10-7BCY29426 8.23 x 10-7BCY29427 1.00 x 10-6BCY25828 4.46 x 10-8BCY25831 3.26 x 10-8BCY28883 8.51 x 10-8 BCY26432 2.89 x 10-7BCY26433 1.89 x 10-7BCY26434 2.25 x 10-7BCY28884 1.38 x 10-8BCY30493 4.16 x 10-7BCY30494 5.94 x 10-7BCY30502 2.07 x 10-7BCY30503 1.72 x 10-7BCY30504 1.98 x 10-7BCY26435 7.42 x 10-7BCY26437 4.25 x 10-7BCY26438 2.23 x 10-7BCY26439 4.66 x 10-7BCY26440 8.37 x 10-7BCY26442 1.09 x 10-6BCY31478 5.77 x 10-7BCY34406 6.89 x 10-7TLR3 Reporter Assay Method Null or TLR3 cells (Invivogen, hkd-htlr3ni) are added to a 96-well plate (5e4 / well) and conditioned with BCY at 37C for 48 hours. Supernatants are collected and mixed with QUANTI-Blue solution (rep-qbs) and read on a plate reader for absorbance (Clariostar) (Dobashi et al (2022) Experimental Biology and Medicine 247(21), 917-922). Selected peptides of the invention were tested in the above mentioned reporter assay and the results are shown in Table 5: Table 5 Average OD630 minus BCY untreated Sample number background size (n) BCY21835 0.101 7 BCY28283 0.055 4 BCY21481 0.531 10 BCY21483 0.433 7 BCY29425 0.166 4 BCY29427 0.052 4 BCY28229 0.079 7 BCY28230 0.116 7 BCY26433 0.048 3 BCY26432 0.108 3 BCY28884 0.836 6 BCY30493 0.126 3 BCY30494 0.129 3 BCY30502 0.194 3 BCY30503 0.278 3 BCY30504 0.223 3 BCY26428 0.137 8 BCY25828 0.131 3 BCY26442 0.112 3 BCY26440 0.122 3 BCY26439 0.644 8 BCY26438 0.889 8 BCY26437 0.201 3 BCY26436 0.120 3 BCY26435 0.148 3 BCY25831 0.217 7 BCY26434 0.177 8 MoMac Cell Binding Assay Method 1. MoMac generation Human PBMCs were isolated from healthy blood donors (the data presented in Table 6 was generated from a single donor referred to as Donor 1875 (230110)) by density gradient centrifugation over Ficoll-Pacque (GE Healthcare 1714403) and Leukosep tubes (Greiner Bio One 227290) and frozen at 5e7 cells / mL. Thawed PBMCs were allowed to adhere to a T175cm flask in RPMI (Gibco 11875-093) 10% FBS (Corning 35-011-CV) and for at least two hours at 37C. Media and unadhered cells were aspirated. Remaining cells (adhered monocytes) were supplemented with 20mL of RPMI+10%FBS+ 100ng / mL M-CSF (Peprotech 300-25) and incubated for 7 days at 37C for differentiation to monocyte derived macrophages, with a re-feed of RPMI+10%FBS+ 100ng / mL M-CSF at day 5. At day 7-10, monocyte derived macrophages (moMacs) were harvested by rinsing with cold PBS and gentle scraping with a sponge cell scraper. Cells were plated in a 96-well round bottom plate at 100,000 cells per well in 100uL RPMI +10%FBS and rested for at least one hour in preparation for binding or activation assays. 2. MoMac cell binding Differentiated moMacs are plated at 100,000 cells per well in 100uL of RPMI + 10% FBS media in a 96-well round bottom plate. Cells are stained with viability dye, incubated for 10 minutes at room temperature and washed. Biotin labelled Bicycle multimer compounds are pre-incubated with equimolar concentration of phycoerythrin labelled streptavidin for 30 minutes at room temperature. After pre-incubation the multimer complex and surface expression antibodies (CD206, TLR3) and antibody control stains are added to the plated moMacs and incubated for 90 minutes on ice to prevent internalization. The supernatant is aspirated by flicking and cells are resuspended in 200uL / well of FACS buffer (PBS + 2% FBS, 0.5M EDTA) and immediately analyzed on Attune Nxt Flow Cytometer without fixation. Selected peptides of the invention were tested in the above mentioned MoMac cell binding assay and the results are shown in Table 6:

[0004] Table 6 conc @ max gMFI max untreated (μM) gMFI gMFI Binding TLR3 TLR3 BCY Summary Fam Epitope Donor 1875 (230110) BCY28217 No 6 3BCY28218 Yes 12 4 1 27790 4552 BCY28219 Yes 1 1 1 8235 4552 BCY28220 Yes 2 1 1 10700 4552 BCY28885 Yes 5 2 1 110982 4552 BCY28887 Yes 7 2 1 125637 4552 BCY28221 No 1nb 1nb 10 7902 4552 The results presented in Table 6 demonstrate that an increase in ³max gMFI´ over the ³untreated J0),´^shows that the multimeric binding complexes have bound. For example, the higher the signal, the more multimeric binding complex has bound. It should be noted that the ³untreated gMFI´^YDOXHV^DUH^DOO^WKH^VDPH because all of the multimeric binding complexes have bound to this single sample. BCY28217 and BCY28221 are non-binding controls. Monocyte-Derived Macrophage Imaging Analysis Monocyte-derived macrophages, generated by negative magnetic-bead enrichment of monocytes from human PBMC followed by M-CSF differentiation, were incubated in the absence (vehicle (BCY), DMSO 0.01%; vehicle (LPS / Poly-IC), 1% dH2O) or presence of / 36^^^^^^QJ^P / ^^^+0:^9DFFLJUDGH^3RO\^,^&^^^^^^J^mL), or non-conjugated bicycle peptides (1000 nM), and the absence or presence of latex beads for 90 min at 37°C. After this time, cells were fixed / permeabilized and labelled with phospho-NF-kB antibody overnight at 4 °C, followed by labelling with AF647-conjugated secondary antibody and Hoechst. Images were acquired by confocal microscopy and are presented herein as Figure 1. NF-kB translocation is known to be an important step in downstream signaling of TLR3. The data presented in Figure 1 demonstrates an increased level of NF-Kb translocation above background for the bicyclic peptide BCY26435 and crucially not for the non-binding bicyclic peptide control. Therefore, this data provides evidence that BCY26435 not only binds to TLR3 but also signals through TLR3. This provides confirmation that BCY26435, and by extrapolation other TLR3 binding bicyclic peptides described herein, have biological function in primary cells.^ The following are numbered aspects of the invention: 1. A peptide ligand capable of binding TLR3, wherein the peptide ligand comprises an amino acid sequence selected from: C-X1-X2-X3-C-X4-X5-X6-X7-X8-X9-C (SEQ ID NO: 1); C-X10-X11-Y-Y-C-X12-Q-T-X13-X14-F-C (SEQ ID NO: 2); X15-X16-X17-X18-X19-X20-X21-X22-X23-X24-X25-X26-X27-X28-X29(SEQ ID NO: 3); C-Q-P-T-X30-X31-C-X32-X33-X34-X35-X36-X37-C (SEQ ID NO: 4); C-Y-Y-X38-X39-X40-Y-A-C-L-D-C (SEQ ID NO: 5); and X41-X42-X43-X44-X45-X46-X47-X48-X49-C-X50-X51-X52-X53-X54(SEQ ID NO: 6); wherein: X1represents D, N, P, Y, 26DiMeTyr, 2FTyr, 3FTyr, or 4FPhe; X2represents A, I, N, P, S, T, Aze, Cba, Cis-HyP, tBuAla, or tBuGly; X3represents A, G, N, P, Q, R, Aib, Aze, Cis-HyP, dA, HyP, or Pip; X4represents L, S, or Cba; X5represents K, P, R, W, 5FTrp, 5MeOTrp, 6ClTrp, 6FTrp, 6MeTrp, Agb, HArg, Trp(Me), or Trp(S); X6represents M, R, or HArg; X7represents A, F, Q, Y, 2FTyr, 3FTyr, 3tBuTyr, or 4FPhe; X8represents H, I, N, V, Cbg, His1Me, His3Me, or tBuGly; X9represents D, F, L, 1Nal, 2Nal, 4tBuPhe, Cba, or tBuAla; X10represents S or T; X11represents K or S; X12represents E or Q; X13represents R or V; X14represents H or R; X15represents C or dC; X16represents A, D, H, I, L, M, N, P, S, T, W, CF3Nva, dP, HyP, Nle, Nva, or TfNle; X17represents E, L, N, P, Q, S, T, Y, 26DiMeTyr, Cba, dL, or tBuAla; X18represents D, E, L, P, R, T, Agb, Cba, Cit, dD, HArg, or tBuAla; X19represents A, E, I, L, M, Q, V, AlloIle, Cba, CF3Ala, dL, HLeu, Nle, or tBuAla; X20represents C or dC; X21represents A, E, F, L, Q, R, T, W, Y, 1Nal, 2FPhe, 2MePhe, 2Nal, 3FPhe, 3MePhe, 4FPhe, 4MePhe, or dE; X22represents A, R, V, Y, 26DiMeTyr, 2FTyr, 3FTyr, 3tBuTyr, 4FPhe, DOPA, or dY; X23represents A, D, W, 1Nal, 2Nal, 4MeoTrp, 5FTrp, dW, Gla, or Trp(S); X24represents A, D, E, H, M, Q, S, Y, dS, K(PYA), or Nle; X25represents E, F, L, N, S, T, V, Cba, or dS; X26represents R, W, Y, 1Nal, 2FTyr, 2MeTrp, 2Nal, 3FTyr, 4FTrp, 5FTrp, 5MeTrp, 6FTrp, 6MeTrp, 7FTrp, 7MeTrp, Cit, dR, HArg, or Trp(Me); X27represents G, R, S, Agb, Cit, dA, dE, or HArg; X28represents L, P, 44DFP, 4FlPro, Aze, Cba, dL, HyP, Pip, tBuAla, or trans-4FlPro; X29represents C, dC, or Cysam; X30represents P, Cis-HyP, HyP, or Pip; X31represents E, Q, or R; X32represents P, Aze, Cis-HyP, or HyP; X33represents F, Y, 2FTyr, 2Nal, 3FTyr, 4FPhe, or 4tBuPhe; X34represents N, S, or Dap; X35represents T or Dap; X36represents W, 1Nal, 2Nal, 4MeoTrp, 5FTrp, 5MeoTrp, 6ClTrp, 6FTrp, AzaTrp, or Trp(S); X37represents P, Aze, Cis-HyP, HyP, or Pip; X38represents E or P; X39represents D or N; X40represents W or Y; X41represents C or dC; X42represents A, D, E, G, K, N, P, S, T, V, Y, 3HyV, Aib, CF3Ala, dA, Dap, dK(PYA), dS, HSer, or K(PYA); X43represents N, T, or 3HyV; X44represents D, E, P, 4FlPro, Cis-Hyp, HyP, or trans-4FlPro; X45represents A, H, M, Q, S, V, Y, 1Nal, 26DiMeTyr, 2FTyr, 2Nal, 3FTyr, 4FPhe, DOPA, or HSer; X46represents A, E, F, I, M, V, 2FPhe, 4CF3Phe, Cba, CF3Nva, Nle, Nva, tBuAla, or TfNle; X47represents A, E, S, T, W, 1Nal, 2MeTrp, 4FTrp, 4MeTrp, 5FTrp, 5MeTrp, 6FTrp, 6MeTrp, 7FTrp, 7MeTrp, AzaTrp, CF3Ala, or Dap; X48represents K, R, Y, 2FTyr, 3FTyr, Agb, DOPA, HArg, or Orn; X49represents A, D, L, V, W, 1Nal, 2Nal, 3HyV, 4FTrp, 5FTrp, 5MeoTrp, 6FTrp, AzaTrp, C5g, Cbg, tBuGly, or Trp(S); X50 represents E, M, Q, R, S, T, Arg(Me), Dap, HArg, or PG; X51represents A, E, K, M, R, S, T, 3HyV, Cit, HArg, or Orn; X52represents A, G, L, M, N, P, Q, Cba, dA, dK(PYA), K(PYA), Nle, Nva, R- aMeLys(PYA), S-aMeLys(PYA), or tBuAla; X53represents D, I, L, M, V, EPA, Nle, Nva, or tBuGly; and X54represents C, dC, or Cysam; or a modified derivative and / or pharmaceutically acceptable salt thereof. 2. A bicyclic peptide ligand which comprises a peptide ligand according to aspect 1, and a molecular scaffold, wherein the three cysteine or Cysam residues of said peptide ligand form covalent bonds with the molecular scaffold to form two loop sequences. 3. The bicyclic peptide ligand according to aspect 2, wherein the peptide ligand of C-X1-X2-X3- C-X4-X5-X6-X7-X8-X9-C (SEQ ID NO: 1) comprises an amino acid sequence selected from: CDI ACLKM YNFC (SEQ ID NO: 7); CDI GCLR MYNFC (SEQ ID NO: 8); CD[tBuAla]G CLRMY NFC (SEQ ID NO: 9); CD[tBuGly]G CLRMY NFC (SEQ ID NO: 10); CD[Cba]G CLRM YNFC (SEQ ID NO: 11); CDI [dA]CLRM YNFC (SEQ ID NO: 12); CDI [Aib]CLR MYNFC (SEQ ID NO: 13); CDI GC[Cba]R MYNFC (SEQ ID NO: 14): CDI GCL[HArg]M YNFC (SEQ ID NO: 15): CDI GCL[Agb]M YNFC (SEQ ID NO: 16); CDI GCLR MYN[1Nal] C (SEQ ID NO: 17); CDI GCLR MYN[2Nal] C (SEQ ID NO: 18); CDI GCLR MYN[4tBuPhe]C (SEQ ID NO: 19); CDI QCLR MYNFC (SEQ ID NO: 20); CNI QCLR MYNFC (SEQ ID NO: 21); CDI RCLRM YNFC (SEQ ID NO: 22); CDI NCLRM YNFC (SEQ ID NO: 23); CPPG CSPRFH LC (SEQ ID NO: 24); CPPG CSPRY HLC (SEQ ID NO: 25; herein referred to as BCY21542 when complexed with a derivative of TATB which has the following structure: wherein * denotes the point of attachment of the three cysteine residues); CP[Cis-HyP]G CSPRY HLC (SEQ ID NO: 26); CP[Aze]G CSPRYH LC (SEQ ID NO: 27); CPPG CSP[HArg]YHLC (SEQ ID NO: 28); CPPG CSPR[4FPhe]H LC (SEQ ID NO: 29); CPPG CSPR[3tBuTyr]H LC (SEQ ID NO: 30): CPPG CSPR[3FTyr] HLC (SEQ ID NO: 31); CPPG CSPR[2FTyr] HLC (SEQ ID NO: 32); CPPG CSPRY [His1Me]LC (SEQ ID NO: 33); CPPG CSPRY [His3Me]LC (SEQ ID NO: 34); CPPG CSPRY H[tBuAla]C (SEQ ID NO: 35); CPPG CSPRY H[Cba]C (SEQ ID NO: 36); CPPG CSPRY NLC (SEQ ID NO: 37); CYN PCLWR QVDC (SEQ ID NO: 38; herein referred to as BCY21497 when complexed with a tri-substituted 2,4,6-tris(bromomethyl)-s-triazine derivative of TBMT having the following structure: wherein * denotes the point of attachment of the three cysteine residues); CYAP CLWR QVDC (SEQ ID NO: 39); CYN PCLWR AVDC (SEQ ID NO: 40); C[4FPhe]NP CLWRQ VDC (SEQ ID NO: 41); C[26DiMeTyr]N PCLWR QVDC (SEQ ID NO: 42); C[3FTyr]N PCLWRQVDC (SEQ ID NO: 43); C[2FTyr]N PCLWRQVDC (SEQ ID NO: 44); CYN [HyP]CLWR QVDC (SEQ ID NO: 45); CYN [Cis-HyP]CLWRQ VDC (SEQ ID NO: 46); CYN [Aze]C LWRQ VDC (SEQ ID NO: 47); CYN [Pip]CLWRQVD C (SEQ ID NO: 48); CYN PC[Cba]WRQVDC (SEQ ID NO: 49); CYN PCL[6MeTrp]RQVDC (SEQ ID NO: 50); CYN PCL[6FTrp]RQ VDC (SEQ ID NO: 51); CYN PCL[5FTrp]RQ VDC (SEQ ID NO: 52); CYN PCL[6ClTrp]RQV DC (SEQ ID NO: 53); CYN PCL[5MeoTrp]RQVDC (SEQ ID NO: 54); CYN PCL[Trp(S)]RQVDC (SEQ ID NO: 55); CYN PCL[Trp(Me)]RQVD C (SEQ ID NO: 56); CYN PCLWR Q[tBuGly]DC (SEQ ID NO: 57); CYN PCLWR Q[Cbg]DC (SEQ ID NO: 58); CYN PCLWR QID C (SEQ ID NO: 59); CYSP CLWR QVDC (SEQ ID NO: 60); and CYTPC LWRQ VDC (SEQ ID NO: 61), such as: wherein the molecular scaffold is a derivative of TATA which has the following structure: wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of C-X1-X2-X3-C-X4-X5-X6-X7-X8-X9-C (SEQ ID NO: 1) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 7)-A-[Sar6]-[KFl] (herein referred to as BCY15200); A-(SEQ ID NO: 7)-A (herein referred to as BCY15212); A-(SEQ ID NO: 8)-A (herein referred to as BCY15747); A-(SEQ ID NO: 8)-A-[K(PYA)] (herein referred to as BCY19281); A-(SEQ ID NO: 9)-A (herein referred to as BCY17064); A-(SEQ ID NO: 10)-A (herein referred to as BCY17065); A-(SEQ ID NO: 11)-A (herein referred to as BCY17066); A-(SEQ ID NO: 12)-A (herein referred to as BCY17067); A-(SEQ ID NO: 13)-A (herein referred to as BCY17068); A-(SEQ ID NO: 14)-A (herein referred to as BCY17070); A-(SEQ ID NO: 15)-A (herein referred to as BCY17071); A-(SEQ ID NO: 16)-A (herein referred to as BCY17072); A-(SEQ ID NO: 17)-A (herein referred to as BCY17079); A-(SEQ ID NO: 18)-A (herein referred to as BCY17080); A-(SEQ ID NO: 19)-A (herein referred to as BCY17081); A-(SEQ ID NO: 20)-A (herein referred to as BCY16675); A-(SEQ ID NO: 21)-A (herein referred to as BCY16676); A-(SEQ ID NO: 22)-A (herein referred to as BCY16677); and A-(SEQ ID NO: 23)-A (herein referred to as BCY16678); or a modified derivative and / or pharmaceutically acceptable salt thereof, or wherein the molecular scaffold is a derivative of TATB which has the following structure: wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of C-X1-X2-X3-C-X4-X5-X6-X7-X8-X9-C (SEQ ID NO: 1) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 24)-A (herein referred to as BCY16997); A-(SEQ ID NO: 25)-A (herein referred to as BCY18125); A-(SEQ ID NO: 25)-A-[K(PYA)] (herein referred to as BCY19741); A-(SEQ ID NO: 25) (herein referred to as BCY21538); Ac-A-(SEQ ID NO: 25) (herein referred to as BCY21539); (SEQ ID NO: 25)-A (herein referred to as BCY21540); Ac-(SEQ ID NO: 25)-A (herein referred to as BCY21541); Ac-(SEQ ID NO: 25) (herein referred to as BCY21543); Ac-A-(SEQ ID NO: 25)-A (herein referred to as BCY21544); A-(SEQ ID NO: 25)-DKTTV (herein referred to as BCY21769); TVKTP-(SEQ ID NO: 25)-A (herein referred to as BCY21775); A-(SEQ ID NO: 25)-DIHNN (herein referred to as BCY21777); A-(SEQ ID NO: 26)-A (herein referred to as BCY21550); A-(SEQ ID NO: 27)-A (herein referred to as BCY21551); A-(SEQ ID NO: 28)-A (herein referred to as BCY21558); A-(SEQ ID NO: 29)-A (herein referred to as BCY21561); A-(SEQ ID NO: 30)-A (herein referred to as BCY21562); A-(SEQ ID NO: 31)-A (herein referred to as BCY21564); A-(SEQ ID NO: 32)-A (herein referred to as BCY21565); A-(SEQ ID NO: 33)-A (herein referred to as BCY21566); A-(SEQ ID NO: 34)-A (herein referred to as BCY21567); A-(SEQ ID NO: 35)-A (herein referred to as BCY21568); A-(SEQ ID NO: 36)-A (herein referred to as BCY21569); and A-(SEQ ID NO: 37)-A (herein referred to as BCY16998); or a modified derivative and / or pharmaceutically acceptable salt thereof, or wherein the molecular scaffold is a tri-substituted 2,4,6-tris(bromomethyl)-s-triazine derivative of TBMT having the following structure: wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of C-X1-X2-X3-C-X4-X5-X6-X7-X8-X9-C (SEQ ID NO: 1) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 38)-A (herein referred to as BCY18251); A-(SEQ ID NO: 38)-A-[K(PYA)] (herein referred to as BCY19587); A-(SEQ ID NO: 38) (herein referred to as BCY21493); (SEQ ID NO: 38)-A (herein referred to as BCY21495); Ac-(SEQ ID NO: 38) (herein referred to as BCY21498); YYYE W-(SEQ ID NO: 38)-A (herein referred to as BCY21773); A-(SEQ ID NO: 39)-A (herein referred to as BCY21485); A-(SEQ ID NO: 40)-A (herein referred to as BCY21490); A-(SEQ ID NO: 41)-A (herein referred to as BCY21500); A-(SEQ ID NO: 42)-A (herein referred to as BCY21502); A-(SEQ ID NO: 43)-A (herein referred to as BCY21503); A-(SEQ ID NO: 44)-A (herein referred to as BCY21504); A-(SEQ ID NO: 45)-A (herein referred to as BCY21505); A-(SEQ ID NO: 46)-A (herein referred to as BCY21506); A-(SEQ ID NO: 47)-A (herein referred to as BCY21507); A-(SEQ ID NO: 48)-A (herein referred to as BCY21508); A-(SEQ ID NO: 49)-A (herein referred to as BCY21510); A-(SEQ ID NO: 50)-A (herein referred to as BCY21515); A-(SEQ ID NO: 51)-A (herein referred to as BCY21517); A-(SEQ ID NO: 52)-A (herein referred to as BCY21518); A-(SEQ ID NO: 53)-A (herein referred to as BCY21519); A-(SEQ ID NO: 54)-A (herein referred to as BCY21521); A-(SEQ ID NO: 55)-A (herein referred to as BCY21522); A-(SEQ ID NO: 56)-A (herein referred to as BCY21523); A-(SEQ ID NO: 57)-A (herein referred to as BCY21527); A-(SEQ ID NO: 58)-A (herein referred to as BCY21528); A-(SEQ ID NO: 59)-A (herein referred to as BCY19930); A-(SEQ ID NO: 59)-VYNVN (herein referred to as BCY21776 ); A-(SEQ ID NO: 60)-A (herein referred to as BCY19931); and A-(SEQ ID NO: 61)-A (herein referred to as BCY19932); or a modified derivative and / or pharmaceutically acceptable salt thereof. 4. The bicyclic peptide ligand according to aspect 2, wherein the peptide ligand of C-X10-X11- Y-Y-C-X12-Q-T-X13-X14-F-C (SEQ ID NO: 2) comprises an amino acid sequence selected from: CTSYY CEQTRH FC (SEQ ID NO: 62); CTKYY CEQTRH FC (SEQ ID NO: 63); and CSKY YCQQ TVRFC (SEQ ID NO: 64), such as: wherein the molecular scaffold is a tri-substituted 2,4,6-tris(bromomethyl)-s-triazine derivative of TBMT having the following structure: wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of C-X10-X11-Y-Y-C-X12-Q-T-X13-X14-F-C (SEQ ID NO: 2) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 62)-A (herein referred to as BCY17006); A-(SEQ ID NO: 63)-A (herein referred to as BCY18134); A-(SEQ ID NO: 63)-A-[K(PYA] (herein referred to as BCY19746); and A-(SEQ ID NO: 64)-A (herein referred to as BCY17012); or a modified derivative and / or pharmaceutically acceptable salt thereof. 5. The bicyclic peptide ligand according to aspect 2, wherein the peptide ligand of X15-X16-X17- X18-X19-X20-X21-X22-X23-X24-X25-X26-X27-X28-X29(SEQ ID NO: 3) comprises an amino acid sequence selected from: CTNE VCTYWYNRGLC (SEQ ID NO: 65); CAN EVCEYWYNRG LC (SEQ ID NO: 66); CPLD LCEYWSFRGLC (SEQ ID NO: 67); CTNE VCRYWYNRG LC (SEQ ID NO: 68); CDS PVCEYWSFRGLC (SEQ ID NO: 69); CHN EVCEYWSFRG LC (SEQ ID NO: 70); CSN EVCEYWSFRGLC (SEQ ID NO: 71); CSN PVCEYWSFRGLC (SEQ ID NO: 72); CNN PVCEYWSFRG LC (SEQ ID NO: 73); CDN EVCEYWSFRG LC (SEQ ID NO: 74); CTSEV CEYWSFRGLC (SEQ ID NO: 75); CSTLVC QRDQ LYSLC (SEQ ID NO: 76); CHN EVCLYWYNRG LC (SEQ ID NO: 77); CWNPVCE YWYN RGLC (SEQ ID NO: 78); CATLQ CQRD MLYGLC (SEQ ID NO: 79); CSTLVC QRDQ LYGLC (SEQ ID NO: 80); CST[tBuAla]VC QRDQ LYGLC (SEQ ID NO: 81); CST[Cba]V CQRDQ LYGLC (SEQ ID NO: 82); CSTL[tBuAla]C QRDQ LYGLC (SEQ ID NO: 83); CSTLVC QRD[Nle] LYGLC (SEQ ID NO: 84); CSTLVC QRDQ [Cba]YGLC (SEQ ID NO: 85); CSTLVC QRDQ LY[dA]LC (SEQ ID NO: 86); CSTLVC QRDQ LYG[tBuAla]C (SEQ ID NO: 87); CSTLVC QRDQ LYG[Cba]C (SEQ ID NO: 88); CST[tBuAla]VC QRDQ LY[dA]LC (SEQ ID NO: 89); CNP LICQ RDQLYG LC (SEQ ID NO: 90); CI SLACQR DQLYG LC (SEQ ID NO: 91); CSTLEC QRDQ LYGLC (SEQ ID NO: 92); CNTLV CQRDQ LYGLC (SEQ ID NO: 93); CTQLM CQR DQLYGLC (SEQ ID NO: 94); CTELM CQRD QLYGLC (SEQ ID NO: 95); CTE[tBuAla]M CQRD QLY[dA]LC (SEQ ID NO: 96); CTELM CQRD QLY[dA]LC (SEQ ID NO: 97); CTE[tBuAla]M CQRD QLYGLC (SEQ ID NO: 98); CTELAC QRDQ LYGLC (SEQ ID NO: 99); CTEL[Nle] CQR DQLYGLC (SEQ ID NO: 100); CTEL[HLeu]C QRDQ LYGLC (SEQ ID NO: 101); CTELM CQR[Gla]QLYG LC (SEQ ID NO: 102); CTELM CQRD QL[3FTyr]GLC (SEQ ID NO: 103); CTELM CQRD QL[2FTyr]GLC (SEQ ID NO: 104); CAN TVCAYWETRGLC (SEQ ID NO: 105); CAN TVCAY[5FTrp] ETRGLC (SEQ ID NO: 106); CPLD LCEYWSVRGLC (SEQ ID NO: 107); CPLD LCEYWSSRGLC (SEQ ID NO: 108); C[HyP]LDLC EYWS SRGLC (SEQ ID NO: 109); CP[tBuAla]D LCEYWSSRGLC (SEQ ID NO: 110); CP[Cba]D LCEYWSSRGLC (SEQ ID NO: 111); CPLD [AlloIle]CEY WSSR GLC (SEQ ID NO: 112); CPLD [tBuAla]CEYWSSRGLC (SEQ ID NO: 113); CPLD [Cba]CEYWSSRGLC (SEQ ID NO: 114); CPLD VCEYWSSRGLC (SEQ ID NO: 115); CPLD LCE[4FPhe]WS SRGLC (SEQ ID NO: 116); CPLD LCEY[2Nal]S SRGLC (SEQ ID NO: 117); CPLD LCEY[1Nal]S SRGLC (SEQ ID NO: 118); CPLD LCEY[5FTrp]S SRGLC (SEQ ID NO: 119); CPLD LCEY[4MeoTrp]SSRG LC (SEQ ID NO: 120); CPLD LCEY[Trp(S)]SSRGLC (SEQ ID NO: 121); CPLD LCEYWSS[HArg]GLC (SEQ ID NO: 122); CPLD LCEYWSS[Cit]GLC (SEQ ID NO: 123); CPLD LCEYWSSR[dA]LC (SEQ ID NO: 124); CPLD LCEYWSSRG[tBuAla]C (SEQ ID NO: 125); CPLD LCEYWSSRG[Cba]C (SEQ ID NO: 126); [dC][dP][dL][dD][dL][dC][dE][dY][dW] [dS][dS][dR]G[dL][dC] (SEQ ID NO: 127); CP[Cba]D LCEY[5FTrp] SSRGLC (SEQ ID NO: 128); CPLD LCEYW[K(PYA)]SRG LC (SEQ ID NO: 129, herein referred to as BCY21632 when complexed with a derivative of TATA which has the following structure: wherein * denotes the point of attachment of the three cysteine residues); CPLD LCEYW[K(PYA)]SRG L[Cysam] (SEQ ID NO: 130, herein referred to as BCY21637 when complexed with a derivative of TATA which has the following structure: wherein * denotes the point of attachment of the three cysteine residues); CPLD LCEY[5FTrp]E SRGLC (SEQ ID NO: 131); CPN DLCEY[5FTrp] SSRGLC (SEQ ID NO: 132); CPLD LCEY[5FTrp]S SR[dA]LC (SEQ ID NO: 133); CPLD LCEY[5FTrp]S SR[dE]LC (SEQ ID NO: 134); CPLD [tBuAla]CEY[5FTrp]S S[HArg][dA]LC (SEQ ID NO: 135); CP[Cba]D LCEY[5FTrp] SS[HArg][dA]LC (SEQ ID NO: 136); CPN DLCEYWSVRG LC (SEQ ID NO: 137); CI TLQCARD MLYGLC (SEQ ID NO: 138); CSTLQ CERDM LYGLC (SEQ ID NO: 139); CI SLACARD MLYGLC (SEQ ID NO: 140); CSTLQ CQRD MLYGLC (SEQ ID NO: 141); CM YRACWVAEEWRPC (SEQ ID NO: 142); CM YRACYY DHEWRPC (SEQ ID NO: 143); CM YRACFYD DEWR PC (SEQ ID NO: 144); CM YRACAY DDEWRPC (SEQ ID NO: 145); CM YRACFAD DEWR PC (SEQ ID NO: 146); CM YRACFYA DEWR PC (SEQ ID NO: 147); CM YRACFYD AEWR PC (SEQ ID NO: 148); C[Nle] YRACFY DDEWRPC (SEQ ID NO: 149); C[Nva]YRA CFYDDE WRPC (SEQ ID NO: 150); C[TfNle]YRA CFYDDE WRPC (SEQ ID NO: 151); C[CF3Nva]YR ACFYDD EWRP C (SEQ ID NO: 152); CM [26DiMeTyr]RACFYD DEWR PC (SEQ ID NO: 153); CM Y[HArg]A CFYDDE WRPC (SEQ ID NO: 154); CM Y[Agb]ACFYDD EWRP C (SEQ ID NO: 155); CM Y[Cit]ACFYDD EWRP C (SEQ ID NO: 156); CM YR[CF3Ala]CFYDDEWRPC (SEQ ID NO: 157); CM YRAC[1Nal] YDDEWRPC (SEQ ID NO: 158); CM YRAC[2Nal] YDDEWRPC (SEQ ID NO: 159); CM YRAC[4MePhe] YDDEWRPC (SEQ ID NO: 160); CM YRAC[3MePhe] YDDEWRPC (SEQ ID NO: 161); CM YRAC[2MePhe] YDDEWRPC (SEQ ID NO: 162); CM YRAC[4FPhe]YD DEWR PC (SEQ ID NO: 163); CM YRAC[3FPhe]YD DEWR PC (SEQ ID NO: 164); CM YRAC[2FPhe]YD DEWR PC (SEQ ID NO: 165); CM YRACF[4FPhe]DD EWR PC (SEQ ID NO: 166); CM YRACF[3tBuTyr]DD EWRP C (SEQ ID NO: 167); CM YRACF[26DiMeTyr]D DEWR PC (SEQ ID NO: 168); CM YRACF[3FTyr] DDEWRPC (SEQ ID NO: 169); CM YRACF[2FTyr] DDEWRPC (SEQ ID NO: 170); CM YRACF[DOPA]DDE WRPC (SEQ ID NO: 171); CM YRACFYD DE[1Nal]R PC (SEQ ID NO: 172); CM YRACFYD DE[2Nal]R PC (SEQ ID NO: 173); CM YRACFYD DE[4FTrp]R PC (SEQ ID NO: 174); CM YRACFYD DE[5FTrp]R PC (SEQ ID NO: 175); CM YRACFYD DE[6FTrp]R PC (SEQ ID NO: 176); CM YRACFYD DE[7FTrp]R PC (SEQ ID NO: 177); CM YRACFYD DE[Trp(Me)]RPC (SEQ ID NO: 178); CM YRACFYD DE[2MeTrp]RPC (SEQ ID NO: 179); CM YRACFYD DE[5MeTrp]RPC (SEQ ID NO: 180); CM YRACFYD DE[6MeTrp]RPC (SEQ ID NO: 181); CM YRACFYD DE[7MeTrp]RPC (SEQ ID NO: 182); CM YRACFYD DEW[HArg]PC (SEQ ID NO: 183); CM YRACFYD DEW[Agb]P C (SEQ ID NO: 184); CM YRACFYD DEW[Cit]P C (SEQ ID NO: 185); CM YRACFYD DEWR [HyP]C (SEQ ID NO: 186); CM YRACFYD DEWR [Aze]C (SEQ ID NO: 187); CM YRACFYD DEWR [Pip]C (SEQ ID NO: 188); CM YRACFYD DEWR [44DFP]C (SEQ ID NO: 189); CM YRACFYD DEWR [4FlPro]C (SEQ ID NO: 190); CM YRACFYD DEWR [trans-4FlPro]C (SEQ ID NO: 191); C[CF3Nva]YR ACFYDD E[1Nal]RP C (SEQ ID NO: 192); C[CF3Nva]YR AC[4MePhe]Y DDE[1Nal] RPC (SEQ ID NO: 193); CLYR ACFYDDE WRPC (SEQ ID NO: 194); CLYR AC[4MePhe]YD DE[1Nal]R PC (SEQ ID NO: 195); and CHY RACFYDD EWRP C (SEQ ID NO: 196), such as: wherein the molecular scaffold is a derivative of TATA which has the following structure: wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of X15-X16-X17-X18-X19-X20-X21-X22-X23-X24-X25-X26-X27-X28-X29(SEQ ID NO: 3) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 65)-A (herein referred to as BCY15206); A-(SEQ ID NO: 65)-A-[Sar6] [KFl] (herein referred to as BCY15194); Ac-(SEQ ID NO: 66)-A-[K(PYA)] (herein referred to as BCY23135); Ac-(SEQ ID NO: 66)-[K(PYA)] (herein referred to as BCY23136); A-(SEQ ID NO: 66)-A-[K(PYA)] (herein referred to as BCY20791); A-(SEQ ID NO: 67)-A (herein referred to as BCY15808); A-(SEQ ID NO: 68)-A (herein referred to as BCY15810); A-(SEQ ID NO: 69)-A (herein referred to as BCY16655); A-(SEQ ID NO: 70)-A (herein referred to as BCY16656); A-(SEQ ID NO: 71)-A (herein referred to as BCY16657); A-(SEQ ID NO: 72)-A (herein referred to as BCY16658); A-(SEQ ID NO: 73)-A (herein referred to as BCY16659); A-(SEQ ID NO: 74)-A (herein referred to as BCY16660); A-(SEQ ID NO: 75)-A (herein referred to as BCY16661); A-(SEQ ID NO: 76)-A (herein referred to as BCY15207); A-(SEQ ID NO: 76)-A-[Sar6]-[KFl] (herein referred to as BCY15195); A-(SEQ ID NO: 76)-A-[K(PYA)] (herein referred to as BCY15750); A-(SEQ ID NO: 77)-A (herein referred to as BCY15811); A-(SEQ ID NO: 78)-A (herein referred to as BCY15812); A-(SEQ ID NO: 79)-A (herein referred to as BCY15813); A-(SEQ ID NO: 80)-A (herein referred to as BCY15814); A-(SEQ ID NO: 80)-A-[Sar6]-[KFl] (herein referred to as BCY15801); Ac-(SEQ ID NO: 80) (herein referred to as BCY17031); A-(SEQ ID NO: 80)-A-[Sar6]-[K(Ac)] (herein referred to as BCY19384); A-(SEQ ID NO: 80)-AGAA AE (herein referred to as BCY19582); A-(SEQ ID NO: 81)-A (herein referred to as BCY17032); A-(SEQ ID NO: 82)-A (herein referred to as BCY17033); A-(SEQ ID NO: 83)-A (herein referred to as BCY17035); A-(SEQ ID NO: 84)-A (herein referred to as BCY17038); A-(SEQ ID NO: 85)-A (herein referred to as BCY17040); A-(SEQ ID NO: 86)-A (herein referred to as BCY17041); A-(SEQ ID NO: 87)-A (herein referred to as BCY17042); A-(SEQ ID NO: 88)-A (herein referred to as BCY17043); Ac-(SEQ ID NO: 89) (herein referred to as BCY19197); A-(SEQ ID NO: 90)-A (herein referred to as BCY16662); A-(SEQ ID NO: 91)-A (herein referred to as BCY16663); A-(SEQ ID NO: 91)-A-[Sar6]-[KFl] (herein referred to as BCY16639); A-(SEQ ID NO: 92)-A (herein referred to as BCY16664); A-(SEQ ID NO: 93)-A (herein referred to as BCY16665); A-(SEQ ID NO: 94)-A (herein referred to as BCY16666); A-(SEQ ID NO: 95)-A (herein referred to as BCY16667); A-(SEQ ID NO: 95)-A-[Sar6]-[KFl] (herein referred to as BCY16643); A-(SEQ ID NO: 95)-A-[K(PYA)] (herein referred to as BCY17238); Ac-(SEQ ID NO: 95) (herein referred to as BCY19193); A-(SEQ ID NO: 96)-A (herein referred to as BCY19192); Ac-(SEQ ID NO: 96) (herein referred to as BCY19196); Ac-(SEQ ID NO: 97) (herein referred to as BCY19194); Ac-(SEQ ID NO: 98) (herein referred to as BCY19195); Ac-(SEQ ID NO: 99) (herein referred to as BCY19198); Ac-(SEQ ID NO: 100) (herein referred to as BCY19199); Ac-(SEQ ID NO: 101) (herein referred to as BCY19200); Ac-(SEQ ID NO: 102) (herein referred to as BCY19203); Ac-(SEQ ID NO: 103) (herein referred to as BCY19205); Ac-(SEQ ID NO: 104) (herein referred to as BCY19206); A-(SEQ ID NO: 105)-A (herein referred to as BCY15208); A-(SEQ ID NO: 105)-A-[K(PYA)] (herein referred to as BCY15751); A-(SEQ ID NO: 106)-A-[K(PYA)] (herein referred to as BCY21608); A-(SEQ ID NO: 107)-A (herein referred to as BCY15209); A-(SEQ ID NO: 107)-A-[Sar6]-[KFl] (herein referred to as BCY15197); A-(SEQ ID NO: 108)-A (herein referred to as BCY15727); A-(SEQ ID NO: 108)-A-[K(PYA)] (herein referred to as BCY17452); Ac-(SEQ ID NO: 108)-[K(PYA)] (herein referred to as BCY19157); Ac-A-(SEQ ID NO: 108)-A-[K(PYA)] (herein referred to as BCY19158); A-(SEQ ID NO: 108)-A-[Sar6]-[(K(Ac)] (herein referred to as BCY19385); A-(SEQ ID NO: 108)-AGAA AE (herein referred to as BCY19580); A-(SEQ ID NO: 108)-KMTH E (herein referred to as BCY21192); A-(SEQ ID NO: 108)-NDSLN (herein referred to as BCY21193 ); A-(SEQ ID NO: 108)-SVNAN (herein referred to as BCY21194); A-(SEQ ID NO: 108)-QGH TPL (herein referred to as BCY21195); A-(SEQ ID NO: 108)-EMEH SN (herein referred to as BCY21196); MR Q-(SEQ ID NO: 108)-ETP (herein referred to as BCY21197); EHM-(SEQ ID NO: 108)-TQ S (herein referred to as BCY21198); EPKR Q-(SEQ ID NO: 108)-A (herein referred to as BCY21199); ANYA N-(SEQ ID NO: 108)-A (herein referred to as BCY21200); DSFH Q-(SEQ ID NO: 108)-A (herein referred to as BCY21201); MRQ-(SEQ ID NO: 108)-ETP-[K(PYA)] (herein referred to as BCY21993); EPKR Q-(SEQ ID NO: 108)-A-[K(PYA)] (herein referred to as BCY21994); Ac-(SEQ ID NO: 108)-A-[K(PYA)] (herein referred to as BCY23137); Ac-(SEQ ID NO: 108)-E-[K(PYA)] (herein referred to as BCY23174); A-(SEQ ID NO: 108)-E-[K(PYA)] (herein referred to as BCY23179); A-(SEQ ID NO: 109)-A-[K(PYA)] (herein referred to as BCY19159); A-(SEQ ID NO: 110)-A-[K(PYA)] (herein referred to as BCY19161); A-(SEQ ID NO: 111)-A-[K(PYA)] (herein referred to as BCY19162); A-(SEQ ID NO: 112)-A-[K(PYA)] (herein referred to as BCY19163); A-(SEQ ID NO: 113)-A-[K(PYA)] (herein referred to as BCY19164); A-(SEQ ID NO: 114)-A-[K(PYA)] (herein referred to as BCY19165); A-(SEQ ID NO: 115)-A-[K(PYA)] (herein referred to as BCY19166); A-(SEQ ID NO: 116)-A-[K(PYA)] (herein referred to as BCY19167); A-(SEQ ID NO: 117)-A (herein referred to as BCY19170); A-(SEQ ID NO: 117)-A-[K(PYA)] (herein referred to as BCY19284); Ac-(SEQ ID NO: 117)-[K(PYA)] (herein referred to as BCY19995); A-(SEQ ID NO: 118)-A-[K(PYA)] (herein referred to as BCY19171); A-(SEQ ID NO: 119)-A-[K(PYA)] (herein referred to as BCY19177); MRQ-(SEQ ID NO: 119)-ETP-[K(PYA)] (herein referred to as BCY21995); EPKR Q-(SEQ ID NO: 119)-A-[K(PYA)] (herein referred to as BCY21996); MRQ-(SEQ ID NO: 119)-ETP (herein referred to as BCY21997); EPKR Q-(SEQ ID NO: 119)-A (herein referred to as BCY21998); Ac-(SEQ ID NO: 119)-[K(PYA)] (herein referred to as BCY22499); A-(SEQ ID NO: 120)-A-[K(PYA)] (herein referred to as BCY19179); A-(SEQ ID NO: 121)-A-[K(PYA)] (herein referred to as BCY19181); A-(SEQ ID NO: 122)-A-[K(PYA)] (herein referred to as BCY19184); A-(SEQ ID NO: 123)-A-[K(PYA)] (herein referred to as BCY19185); A-(SEQ ID NO: 124)-A-[K(PYA)] (herein referred to as BCY19187); A-(SEQ ID NO: 125)-A-[K(PYA)] (herein referred to as BCY19188); A-(SEQ ID NO: 126)-A-[K(PYA)] (herein referred to as BCY19189); [dA]-(SEQ ID NO: 127)-[dA]-[K(PYA)] (herein referred to as BCY20840); A-(SEQ ID NO: 128)-A-[K(PYA)] (herein referred to as BCY21040); A-(SEQ ID NO: 129)-A (herein referred to as BCY21631); A-(SEQ ID NO: 129) (herein referred to as BCY21633); Ac-(SEQ ID NO: 129) (herein referred to as BCY21634); A-(SEQ ID NO: 130) (herein referred to as BCY21635); Ac-(SEQ ID NO: 130) (herein referred to as BCY21636); Ac-(SEQ ID NO: 131)-[K(PYA)] (herein referred to as BCY23702); Ac-(SEQ ID NO: 132)-[K(PYA)] (herein referred to as BCY23703); Ac-(SEQ ID NO: 132)-[K(PYA)-(Triazolyl)-(PEG)2-methyl] (herein referred to as BCY25601); Ac-(SEQ ID NO: 133)-[K(PYA)] (herein referred to as BCY23704); Ac-(SEQ ID NO: 134)-[K(PYA)] (herein referred to as BCY23705); Ac-(SEQ ID NO: 135)-[K(PYA)] (herein referred to as BCY23706); Ac-(SEQ ID NO: 136)-[K(PYA)] (herein referred to as BCY23707); Ac-(SEQ ID NO: 136)-[K(PYA)-(Triazolyl)-(PEG)2-methyl] (herein referred to as BCY25602); A-(SEQ ID NO: 137)-A (herein referred to as BCY15729); A-(SEQ ID NO: 138)-A (herein referred to as BCY15210); A-(SEQ ID NO: 138)-A-[Sar6] -[KFl] (herein referred to as BCY15198); A-(SEQ ID NO: 138)-A-[K(PYA)] (herein referred to as BCY15752); A-(SEQ ID NO: 139)-A (herein referred to as BCY15731); A-(SEQ ID NO: 139)-A-[Sar6] -[KFl] (herein referred to as BCY15730); A-(SEQ ID NO: 140)-A (herein referred to as BCY15733); A-(SEQ ID NO: 141)-A (herein referred to as BCY15735); and A-(SEQ ID NO: 141)-A-[Sar6] -[KFl] (herein referred to as BCY15734); or a modified derivative and / or pharmaceutically acceptable salt thereof, or wherein the molecular scaffold is a derivative of TATB which has the following structure: wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of X15-X16-X17-X18-X19-X20-X21-X22-X23-X24-X25-X26-X27-X28-X29(SEQ ID NO: 3) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 142)-A (herein referred to as BCY17001); A-(SEQ ID NO: 143)-A (herein referred to as BCY18128); A-(SEQ ID NO: 143)-A-[K(PYA)] (herein referred to as BCY19743); A-(SEQ ID NO: 144)-A (herein referred to as BCY18129); A-(SEQ ID NO: 144)-A-[K(PYA)] (herein referred to as BCY19744); Ac-A-(SEQ ID NO: 144)-A (herein referred to as BCY24131 ); Ac-(SEQ ID NO: 144) (herein referred to as BCY24135); A-(SEQ ID NO: 144) (herein referred to as BCY24450); Ac-A-(SEQ ID NO: 144) (herein referred to as BCY24451); (SEQ ID NO: 144)-A (herein referred to as BCY24452); Ac-(SEQ ID NO: 144)-A (herein referred to as BCY24453); AHG G-(SEQ ID NO: 144)-EVHA (herein referred to as BCY25863 ); AI KP-(SEQ ID NO: 144)-QHEA (herein referred to as BCY25864); ADST-(SEQ ID NO: 144)-QH PA (herein referred to as BCY25865); ALNG-(SEQ ID NO: 144)-PLS A (herein referred to as BCY25866); ALNG-(SEQ ID NO: 144)-PLS A-[K(PYA)] (herein referred to as BCY28840); A-(SEQ ID NO: 145)-A (herein referred to as BCY24442); A-(SEQ ID NO: 146)-A (herein referred to as BCY24443); A-(SEQ ID NO: 147)-A (herein referred to as BCY24444); A-(SEQ ID NO: 148)-A (herein referred to as BCY24445); A-(SEQ ID NO: 149)-A (herein referred to as BCY24456); A-(SEQ ID NO: 150)-A (herein referred to as BCY24457); A-(SEQ ID NO: 151)-A (herein referred to as BCY24458); A-(SEQ ID NO: 152)-A (herein referred to as BCY24459); A-(SEQ ID NO: 153)-A (herein referred to as BCY24462); A-(SEQ ID NO: 154)-A (herein referred to as BCY24466); A-(SEQ ID NO: 155)-A (herein referred to as BCY24467); A-(SEQ ID NO: 156)-A (herein referred to as BCY24468); A-(SEQ ID NO: 157)-A (herein referred to as BCY24469); A-(SEQ ID NO: 158)-A (herein referred to as BCY24471); A-(SEQ ID NO: 159)-A (herein referred to as BCY24472); A-(SEQ ID NO: 160)-A (herein referred to as BCY24473); A-(SEQ ID NO: 161)-A (herein referred to as BCY24474); A-(SEQ ID NO: 162)-A (herein referred to as BCY24475); A-(SEQ ID NO: 163)-A (herein referred to as BCY24477); A-(SEQ ID NO: 164)-A (herein referred to as BCY24478); A-(SEQ ID NO: 165)-A (herein referred to as BCY24479); A-(SEQ ID NO: 166)-A (herein referred to as BCY24480); A-(SEQ ID NO: 167)-A (herein referred to as BCY24481); A-(SEQ ID NO: 168)-A (herein referred to as BCY24482); A-(SEQ ID NO: 169)-A (herein referred to as BCY24483); A-(SEQ ID NO: 170)-A (herein referred to as BCY24484); A-(SEQ ID NO: 171)-A (herein referred to as BCY24485); A-(SEQ ID NO: 172)-A (herein referred to as BCY24486); A-(SEQ ID NO: 173)-A (herein referred to as BCY24487); A-(SEQ ID NO: 174)-A (herein referred to as BCY24488); A-(SEQ ID NO: 175)-A (herein referred to as BCY24489); A-(SEQ ID NO: 176)-A (herein referred to as BCY24490); A-(SEQ ID NO: 177)-A (herein referred to as BCY24491); A-(SEQ ID NO: 178)-A (herein referred to as BCY24492); A-(SEQ ID NO: 179)-A (herein referred to as BCY24493); A-(SEQ ID NO: 180)-A (herein referred to as BCY24495); A-(SEQ ID NO: 181)-A (herein referred to as BCY24496); A-(SEQ ID NO: 182)-A (herein referred to as BCY24497); A-(SEQ ID NO: 183)-A (herein referred to as BCY24498); A-(SEQ ID NO: 184)-A (herein referred to as BCY24499); A-(SEQ ID NO: 185)-A (herein referred to as BCY24500); A-(SEQ ID NO: 186)-A (herein referred to as BCY24501); A-(SEQ ID NO: 187)-A (herein referred to as BCY24503); A-(SEQ ID NO: 188)-A (herein referred to as BCY24504); A-(SEQ ID NO: 189)-A (herein referred to as BCY24505); A-(SEQ ID NO: 190)-A (herein referred to as BCY24506); A-(SEQ ID NO: 191)-A (herein referred to as BCY24509); ALNG-(SEQ ID NO: 192)-PLS A (herein referred to as BCY28838); ALNG-(SEQ ID NO: 192)-PLS A-[K(PYA)] (herein referred to as BCY28841); ALNG-(SEQ ID NO: 193)-PLS A (herein referred to as BCY28839); ALNG-(SEQ ID NO: 193)-PLS A-[K(PYA)] (herein referred to as BCY28842); ALEQ N-(SEQ ID NO: 194)-A (herein referred to as BCY25861); ALEQ N-(SEQ ID NO: 194)-A-[K(PYA)] (herein referred to as BCY28843); ALEQ N-(SEQ ID NO: 195)-A (herein referred to as BCY28844 ); ALEQ N-(SEQ ID NO: 195)-A-[K(PYA)] (herein referred to as BCY28845); and AHAG T-(SEQ ID NO: 196)-A (herein referred to as BCY25859 ); or a modified derivative and / or pharmaceutically acceptable salt thereof. 6. The bicyclic peptide ligand according to aspect 2, wherein the peptide ligand of C-Q-P-T- X30-X31-C-X32-X33-X34-X35-X36-X37-C (SEQ ID NO: 4) comprises an amino acid sequence selected from: CQ PTPRCPFSTWPC (herein referred to as SEQ ID NO: 197); CQ PTPQCPY STWPC (herein referred to as SEQ ID NO: 198, herein referred to as BCY20723 when complexed with a derivative of TATB which has the following structure: wherein * denotes the point of attachment of the three cysteine residues); CQ PT[HyP]QCPY STWPC (herein referred to as SEQ ID NO: 199); CQ PT[Cis-HyP]QCPYS TWPC (herein referred to as SEQ ID NO: 200); CQ PT[Pip]QC PYSTWPC (herein referred to as SEQ ID NO: 201); CQ PTPECPYS TWPC (herein referred to as SEQ ID NO: 202); CQ PTPQC[HyP]Y STWPC (herein referred to as SEQ ID NO: 203); CQ PTPQC[Cis-HyP]YS TWPC (herein referred to as SEQ ID NO: 204); CQ PTPQC[Aze]YSTWPC (herein referred to as SEQ ID NO: 205); CQ PTPQCP[2Nal] STWPC (herein referred to as SEQ ID NO: 206); CQ PTPQCP[4tBuPhe]STWPC (herein referred to as SEQ ID NO: 207); CQ PTPQCP[4FPhe]S TWPC (herein referred to as SEQ ID NO: 208); CQ PTPQCP[3FTyr] STWP C (herein referred to as SEQ ID NO: 209); CQ PTPQCP[2FTyr] STWP C (herein referred to as SEQ ID NO: 210); CQ PTPQCPY [Dap]TWPC (herein referred to as SEQ ID NO: 211); CQ PTPQCPY S[Dap]WPC (herein referred to as SEQ ID NO: 212); CQ PTPQCPY ST[2Nal]PC (herein referred to as SEQ ID NO: 213); CQ PTPQCPY ST[1Nal]PC (herein referred to as SEQ ID NO: 214); CQ PTPQCPY ST[6FTrp]PC (herein referred to as SEQ ID NO: 215); CQ PTPQCPY ST[5FTrp]PC (herein referred to as SEQ ID NO: 216); CQ PTPQCPY ST[6ClTrp]PC (herein referred to as SEQ ID NO: 217); CQ PTPQCPY ST[4MeoTrp]P C (herein referred to as SEQ ID NO: 218); CQ PTPQCPY ST[5MeoTrp]P C (herein referred to as SEQ ID NO: 219); CQ PTPQCPY ST[Trp(S)]PC (herein referred to as SEQ ID NO: 220); CQ PTPQCPY ST[AzaTrp]PC (herein referred to as SEQ ID NO: 221); CQ PTPQCPY STW[HyP]C (herein referred to as SEQ ID NO: 222); CQ PTPQCPY STW[Cis-HyP]C (herein referred to as SEQ ID NO: 223); CQ PTPQCPY STW[Aze]C (herein referred to as SEQ ID NO: 224); CQ PTPQCPY STW[Pip] C (herein referred to as SEQ ID NO: 225); and CQ PTPECPYN TWPC (herein referred to as SEQ ID NO: 226), such as wherein the molecular scaffold is a derivative of TATB which has the following structure: wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of C-Q-P-T-X30-X31-C-X32-X33-X34-X35-X36-X37-C (SEQ ID NO: 4) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 197)-A (herein referred to as BCY16999); A-(SEQ ID NO: 197)-A-[K(PYA)] (herein referred to as BCY17693); A-(SEQ ID NO: 197)-A-[Sar6]-[K(Ac)] (herein referred to as BCY19387); A-(SEQ ID NO: 198)-A (herein referred to as BCY18126); Ac-A-(SEQ ID NO: 198)-A (herein referred to as BCY20725); A-(SEQ ID NO: 198)-NLNLK (herein referred to as BCY21770 ); VNEN I-(SEQ ID NO: 198)-A (herein referred to as BCY21771); A-(SEQ ID NO: 198)-RNPH D (herein referred to as BCY21772); A-(SEQ ID NO: 198)-IHN NG (herein referred to as BCY21774); TNEG I-(SEQ ID NO: 198)-A (herein referred to as BCY21778); VNEN I-(SEQ ID NO: 198)-A-[K(PYA)] (herein referred to as BCY23767); A-(SEQ ID NO: 199)-A (herein referred to as BCY20731); A-(SEQ ID NO: 200)-A (herein referred to as BCY20732); A-(SEQ ID NO: 201)-A (herein referred to as BCY20734); A-(SEQ ID NO: 202)-A (herein referred to as BCY20735); A-(SEQ ID NO: 203)-A (herein referred to as BCY20736); A-(SEQ ID NO: 204)-A (herein referred to as BCY20737); A-(SEQ ID NO: 205)-A (herein referred to as BCY20738); A-(SEQ ID NO: 206)-A (herein referred to as BCY20741); A-(SEQ ID NO: 207)-A (herein referred to as BCY20742); A-(SEQ ID NO: 208)-A (herein referred to as BCY20743); A-(SEQ ID NO: 209)-A (herein referred to as BCY20746); A-(SEQ ID NO: 210)-A (herein referred to as BCY20747); A-(SEQ ID NO: 211)-A (herein referred to as BCY20748); A-(SEQ ID NO: 212)-A (herein referred to as BCY20749); A-(SEQ ID NO: 213)-A (herein referred to as BCY20751); A-(SEQ ID NO: 214)-A (herein referred to as BCY20752); A-(SEQ ID NO: 215)-A (herein referred to as BCY20756); A-(SEQ ID NO: 216)-A (herein referred to as BCY20757); A-(SEQ ID NO: 217)-A (herein referred to as BCY20758); A-(SEQ ID NO: 218)-A (herein referred to as BCY20759); A-(SEQ ID NO: 219)-A (herein referred to as BCY20760); A-(SEQ ID NO: 220)-A (herein referred to as BCY20761); A-(SEQ ID NO: 221)-A (herein referred to as BCY20762); A-(SEQ ID NO: 222)-A (herein referred to as BCY20763); A-(SEQ ID NO: 223)-A (herein referred to as BCY20764); A-(SEQ ID NO: 224)-A (herein referred to as BCY20765); A-(SEQ ID NO: 225)-A (herein referred to as BCY20766); A-(SEQ ID NO: 226)-A (herein referred to as BCY18127); and A-(SEQ ID NO: 226)-A-[K(PYA)] (herein referred to as BCY19742); or a modified derivative and / or pharmaceutically acceptable salt thereof. 7. The bicyclic peptide ligand according to aspect 2, wherein the peptide ligand of C-Y-Y-X38- X39-X40-Y-A-C-L-D-C (SEQ ID NO: 5) comprises an amino acid sequence selected from: CYYP DYYACLD C (herein referred to as SEQ ID NO: 227); CYYE NYYACLD C (herein referred to as SEQ ID NO: 228); and CYYP DWYA CLDC (herein referred to as SEQ ID NO: 229), such as wherein the molecular scaffold is a tri-substituted 2,4,6-tris(bromomethyl)-s-triazine derivative of TBMT having the following structure: wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of C-Y-Y-X38-X39-X40-Y-A-C-L-D-C (SEQ ID NO: 5) additionally comprises N- and / or C- terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 227)-A (herein referred to as BCY17007); A-(SEQ ID NO: 228)-A (herein referred to as BCY18135); A-(SEQ ID NO: 229)-A (herein referred to as BCY18136); and A-(SEQ ID NO: 229)-A-[K(PYA)] (herein referred to as BCY19747); or a modified derivative and / or pharmaceutically acceptable salt thereof. 8. The bicyclic peptide ligand according to aspect 2, wherein the peptide ligand of X41-X42- X43-X44-X45-X46-X47-X48-X49-C-X50-X51-X52-X53-X54(SEQ ID NO: 6) comprises an amino acid sequence selected from: CNN PVMTYWCTKG IC (herein referred to as SEQ ID NO: 230); CNN PVMTYWCEKG IC (herein referred to as SEQ ID NO: 231); CDN EVITYWCTKG IC (herein referred to as SEQ ID NO: 232); CDN EV[tBuAla]TYWCTKGI C (herein referred to as SEQ ID NO: 233); CDN EVFTYWCTKGI C (herein referred to as SEQ ID NO: 234); CDN EV[Cba]TYWCTKGI C (herein referred to as SEQ ID NO: 235); CDN EVITY[2Nal] CTKG IC (herein referred to as SEQ ID NO: 236); CDN EVITY[1Nal] CTKG IC (herein referred to as SEQ ID NO: 237); CDN EVITYWCT[Orn]GI C (herein referred to as SEQ ID NO: 238); CDN EVITYWCT[HArg]GI C (herein referred to as SEQ ID NO: 239); CDN EVITYWCTK[dA]I C (herein referred to as SEQ ID NO: 240); CDN EVITYWCTKG [tBuGly]C (herein referred to as SEQ ID NO: 241); CDN EVIT[DOPA]WCTKGI C (herein referred to as SEQ ID NO: 242); CDN PVFTYWCTKGI C (herein referred to as SEQ ID NO: 243); CNN PVMAY WCTKG IC (herein referred to as SEQ ID NO: 244); CPN PVITYWCTKG IC (herein referred to as SEQ ID NO: 245); CDN EVITYWCQ MGVC (herein referred to as SEQ ID NO: 246); CDN EVITYWCQ RGVC (herein referred to as SEQ ID NO: 247); CDN EVITYWCM RGI C (herein referred to as SEQ ID NO: 248); CDN EVITYWCQ RGIC (herein referred to as SEQ ID NO: 249); CDN EVITY[6FTrp] CQR GIC (herein referred to as SEQ ID NO: 250); CDN EVITY[5FTrp] CQR GIC (herein referred to as SEQ ID NO: 251); CDN EVITY[5MeoTrp]CQ RGI C (herein referred to as SEQ ID NO: 252); CDN EVITY[Trp(S)]CQ RGI C (herein referred to as SEQ ID NO: 253); CDN EVITY[AzaTrp] CQR GIC (herein referred to as SEQ ID NO: 254); CDN EVITYWCQ [HArg]G IC (herein referred to as SEQ ID NO: 255); CDN EVITYWCQ [Cit]G IC (herein referred to as SEQ ID NO: 256); CDN EVFEYWCTKGI C (herein referred to as SEQ ID NO: 257); CDN EVITYWCER GIC (herein referred to as SEQ ID NO: 258); CDN EVITYWCEM GIC (herein referred to as SEQ ID NO: 259); CSN PVFAYWCSRQM C (herein referred to as SEQ ID NO: 260); CSN PVFAYWCERGI C (herein referred to as SEQ ID NO: 261, herein referred to as BCY21615 when complexed with a tri-substituted 2,4,6-tris(bromomethyl)-s-triazine derivative of TBMT having the following structure: wherein * denotes the point of attachment of the three cysteine residues); CSN PVFAYWCER[K(PYA)]IC (herein referred to as SEQ ID NO: 262); CSN PVFAYWCER[dK(PYA)]IC (herein referred to as SEQ ID NO: 263); CSN PVFAYWCER[S-aMeLys(PYA)]I C (herein referred to as SEQ ID NO: 264); CSN PVFAYWCER[R-aMeLys(PYA)]I C (herein referred to as SEQ ID NO: 265); C[K(PYA)]NPVFAY WCER GIC (herein referred to as SEQ ID NO: 266); CSN PVFAY[5FTrp] CERGI C (herein referred to as SEQ ID NO: 267); CSN PVFAYWCERGI [Cysam] (herein referred to as SEQ ID NO: 268, herein referred to as BCY21623 when complexed with a tri-substituted 2,4,6-tris(bromomethyl)-s-triazine derivative of TBMT having the following structure: wherein * denotes the point of attachment of the three cysteine residues); C[K(PYA)]NPVFAY WCER GI[Cysam] (herein referred to as SEQ ID NO: 269); CSN PVFAYWC[Dap]RGI C (herein referred to as SEQ ID NO: 270); CKN PVFAYWC[PG]RG IC (herein referred to as SEQ ID NO: 271); CEN PVFAYWCERGI C (herein referred to as SEQ ID NO: 272); C[dA]NP VFAYWCERGI C (herein referred to as SEQ ID NO: 273); CG NPVFAYWCERG IC (herein referred to as SEQ ID NO: 274); C[Aib] NPVFAYWCERG IC (herein referred to as SEQ ID NO: 275); CSN [trans-4FlPro]VFAYWCERG IC (herein referred to as SEQ ID NO: 276); CSN [4FlPro]V FAYWC ERGI C (herein referred to as SEQ ID NO: 277); CSN [HyP]VFAYWCERGI C (herein referred to as SEQ ID NO: 278); CSN [Cis-HyP]VFAYWCERGI C (herein referred to as SEQ ID NO: 279); CSN P[HSer]FA YWCE RGI C (herein referred to as SEQ ID NO: 280); CSN PV[2FPhe]AYWCERG IC (herein referred to as SEQ ID NO: 281); CSN PV[4CF3Phe]AYWCERG IC (herein referred to as SEQ ID NO: 282); CSN PVFSYWCERGI C (herein referred to as SEQ ID NO: 283); CSN PVF[Dap]YWCERGI C (herein referred to as SEQ ID NO: 284); CSN PVF[CF3Ala]Y WCER GIC (herein referred to as SEQ ID NO: 285); CSN PVFA[2FTyr]WCERG IC (herein referred to as SEQ ID NO: 286); CSN PVFA[3FTyr]WCERG IC (herein referred to as SEQ ID NO: 287); CSN PVFAY[4FTrp] CERGI C (herein referred to as SEQ ID NO: 288); CSN PVFAYWCE[Cit]GI C (herein referred to as SEQ ID NO: 289); CSN PVFAYWCER[dA]I C (herein referred to as SEQ ID NO: 290); CSN PVFAYWCERG[Nva]C (herein referred to as SEQ ID NO: 291); CSN PVFAYWCERG[Nle] C (herein referred to as SEQ ID NO: 292); CSN PVFAYWCERG[EPA] C (herein referred to as SEQ ID NO: 293); CSN PVFAYWCERG[tBuGly] C (herein referred to as SEQ ID NO: 294); CSN [4FlPro]V FAY[5FTrp]C ERG[EPA] C (herein referred to as SEQ ID NO: 295); C[Aib] N[4FlPro]VFAY[5FTrp] CERG[EPA] C (herein referred to as SEQ ID NO: 296); C[dS]N[4FlPro]V FAY[5FTrp]CE RG[EPA]C (herein referred to as SEQ ID NO: 297); C[K(PYA)]N[4FlPro]VFAY[5FTrp] CERG [EPA]C (herein referred to as SEQ ID NO: 298); C[dK(PYA)]N[4FlPro]VFAY[5FTrp] CERG [EPA]C (herein referred to as SEQ ID NO: 299); [dC]SN[4FlPro]V FAY[5FTrp]CE RG[EPA]C (herein referred to as SEQ ID NO: 300); CSN [4FlPro]V FAY[5FTrp]C ERG[EPA] [dC] (herein referred to as SEQ ID NO: 301); [dC]SN[4FlPro]V FAY[5FTrp]CE RG[EPA][dC] (herein referred to as SEQ ID NO: 302); CSN PVFAYWCSRNLC (herein referred to as SEQ ID NO: 303); CSN PVFAYWCSRGLC (herein referred to as SEQ ID NO: 304); CTTDM MWKVCRTLD C (herein referred to as SEQ ID NO: 305); CATD HMWKVCRTLDC (herein referred to as SEQ ID NO: 306); CKTD AMWKVCRTLDC (herein referred to as SEQ ID NO: 307); CSTD QMWKVCRTLD C (herein referred to as SEQ ID NO: 308); CSTD YMWKVCRTLDC (herein referred to as SEQ ID NO: 309, herein referred to as BCY23141 when complexed with a tri-substituted 2,4,6-tris(bromomethyl)-s-triazine derivative of TBMT having the following structure: wherein * denotes the point of attachment of the three cysteine residues); CSTD Y[Nle]WKVCRTLD C (herein referred to as SEQ ID NO: 310); CATD YMWKVCRTLDC (herein referred to as SEQ ID NO: 311); CSTD AMWKVCRTLDC (herein referred to as SEQ ID NO: 312); CSTD YAWKV CRTLDC (herein referred to as SEQ ID NO: 313); CSTD YMWKACRTLDC (herein referred to as SEQ ID NO: 314); CSTD YMWKVCRALD C (herein referred to as SEQ ID NO: 315); CSTD YMWKVCRTAD C (herein referred to as SEQ ID NO: 316); C[CF3Ala]TDYMWKVC RTLDC (herein referred to as SEQ ID NO: 317); C[HSer]TDYM WKVC RTLDC (herein referred to as SEQ ID NO: 318); CTTDY MWK VCRTLDC (herein referred to as SEQ ID NO: 319); C[3HyV]TDY MWKVCRTLDC (herein referred to as SEQ ID NO: 320); CS[3HyV]D YMWKVCRTLD C (herein referred to as SEQ ID NO: 321); C[Dap]TDY MWKVCRTLDC (herein referred to as SEQ ID NO: 322); CSTD [4FPhe]MWK VCRTLDC (herein referred to as SEQ ID NO: 323); CSTD [1Nal]MWKVCR TLDC (herein referred to as SEQ ID NO: 324); CSTD [2Nal]MWKVCR TLDC (herein referred to as SEQ ID NO: 325); CSTD [26DiMeTyr]MWKVCRTLDC (herein referred to as SEQ ID NO: 326); CSTD [3FTyr]MWKVCRTLD C (herein referred to as SEQ ID NO: 327); CSTD [2FTyr]MWKVCRTLD C (herein referred to as SEQ ID NO: 328); CSTD [DOPA]M WKVC RTLDC (herein referred to as SEQ ID NO: 329); CSTD Y[Nva]WKVC RTLDC (herein referred to as SEQ ID NO: 330); CSTD Y[TfNle]WKVC RTLDC (herein referred to as SEQ ID NO: 331); CSTD YEWKV CRTLDC (herein referred to as SEQ ID NO: 332); CSTD Y[CF3Nva]WKV CRTLDC (herein referred to as SEQ ID NO: 333); CSTD YM[1Nal] KVCRTLDC (herein referred to as SEQ ID NO: 334); CSTD YM[4FTrp]K VCRTLDC (herein referred to as SEQ ID NO: 335); CSTD YM[5FTrp]K VCRTLDC (herein referred to as SEQ ID NO: 336); CSTD YM[6FTrp]K VCRTLDC (herein referred to as SEQ ID NO: 337); CSTD YM[7FTrp]K VCRTLDC (herein referred to as SEQ ID NO: 338); CSTD YM[2MeTrp]KVCRTLD C (herein referred to as SEQ ID NO: 339); CSTD YM[4MeTrp]KVCRTLD C (herein referred to as SEQ ID NO: 340); CSTD YM[5MeTrp]KVCRTLD C (herein referred to as SEQ ID NO: 341); CSTD YM[6MeTrp]KVCRTLD C (herein referred to as SEQ ID NO: 342); CSTD YM[7MeTrp]KVCRTLD C (herein referred to as SEQ ID NO: 343); CSTD YM[AzaTrp]K VCRTLDC (herein referred to as SEQ ID NO: 344); CSTD YMW[HArg]VC RTLDC (herein referred to as SEQ ID NO: 345); CSTD YMW[Orn]VC RTLDC (herein referred to as SEQ ID NO: 346); CSTD YMW[Agb]VCRTLDC (herein referred to as SEQ ID NO: 347); CSTD YMWK[tBuGly]CRTLDC (herein referred to as SEQ ID NO: 348); CSTD YMWK[Cbg]CRTLDC (herein referred to as SEQ ID NO: 349); CSTD YMWK[C5g]CRTLDC (herein referred to as SEQ ID NO: 350); CSTD YMWK[3HyV]CRTLDC (herein referred to as SEQ ID NO: 351); CSTD YMWKVC[HArg]TLDC (herein referred to as SEQ ID NO: 352); CSTD YMWKVC[Arg(Me)]TLDC (herein referred to as SEQ ID NO: 353); CSTD YMWKVCR[3HyV]LD C (herein referred to as SEQ ID NO: 354); CSTD YMWKVCRT[tBuAla]DC (herein referred to as SEQ ID NO: 355); CSTD YMWKVCRT[Cba]D C (herein referred to as SEQ ID NO: 356); CSTD YMWKVCRT[Nva]DC (herein referred to as SEQ ID NO: 357); CSTD YMWKVCRT[Nle] DC (herein referred to as SEQ ID NO: 358); CTTDM AWR DCRTLDC (herein referred to as SEQ ID NO: 359); CTTDM AWR LCRTLDC (herein referred to as SEQ ID NO: 360); CTTDM VWK VCRTLDC (herein referred to as SEQ ID NO: 361); CVTD YMWKVCRTLDC (herein referred to as SEQ ID NO: 362); CYTD SMWKVCRTLDC (herein referred to as SEQ ID NO: 363); CTTDM MWKVCREP DC (herein referred to as SEQ ID NO: 364); CTTDM MWKVCRSM DC (herein referred to as SEQ ID NO: 365); and CTTDMMWKVCRTLDC (herein referred to as SEQ ID NO: 366), such as wherein the molecular scaffold is a derivative of TATA which has the following structure: wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of X41-X42-X43-X44-X45-X46-X47-X48-X49-C-X50-X51-X52-X53-X54(SEQ ID NO: 6) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 230)-A (herein referred to as BCY15211); A-(SEQ ID NO: 230)-A-[Sar6]-[KFl] (herein referred to as BCY15199); A-(SEQ ID NO: 231)-A (herein referred to as BCY15737); A-(SEQ ID NO: 232)-A (herein referred to as BCY15739); A-(SEQ ID NO: 232)-A-[Sar6]-[KFl] (herein referred to as BCY15738); A-(SEQ ID NO: 232)-A-[Sar6]-[K(Ac)] (herein referred to as BCY19386); A-(SEQ ID NO: 232)-AGAA AE (herein referred to as BCY19581); A-(SEQ ID NO: 233)-A (herein referred to as BCY17047); A-(SEQ ID NO: 234)-A (herein referred to as BCY17049); A-(SEQ ID NO: 235)-A (herein referred to as BCY17051); A-(SEQ ID NO: 236)-A (herein referred to as BCY17055); A-(SEQ ID NO: 237)-A (herein referred to as BCY17056); A-(SEQ ID NO: 238)-A (herein referred to as BCY17057); A-(SEQ ID NO: 239)-A (herein referred to as BCY17058); A-(SEQ ID NO: 240)-A (herein referred to as BCY17059); A-(SEQ ID NO: 241)-A (herein referred to as BCY17061); A-(SEQ ID NO: 242)-A (herein referred to as BCY17656); A-(SEQ ID NO: 243)-A (herein referred to as BCY15741); A-(SEQ ID NO: 244)-A (herein referred to as BCY15743); A-(SEQ ID NO: 245)-A (herein referred to as BCY15745); A-(SEQ ID NO: 246)-A (herein referred to as BCY16668); A-(SEQ ID NO: 247)-A (herein referred to as BCY16669); A-(SEQ ID NO: 248)-A (herein referred to as BCY16670); A-(SEQ ID NO: 249)-A (herein referred to as BCY16671); A-(SEQ ID NO: 249)-A-[Sar6]-[KFl] (herein referred to as BCY16647); Ac-A-(SEQ ID NO: 249)-A (herein referred to as BCY19586 ); A-(SEQ ID NO: 250)-A (herein referred to as BCY18510); A-(SEQ ID NO: 251)-A (herein referred to as BCY18511); A-(SEQ ID NO: 251)-A-[K(PYA)] (herein referred to as BCY25826); A-(SEQ ID NO: 252)-A (herein referred to as BCY18514); A-(SEQ ID NO: 253)-A (herein referred to as BCY18515); A-(SEQ ID NO: 254)-A (herein referred to as BCY18518); A-(SEQ ID NO: 255)-A (herein referred to as BCY18519); A-(SEQ ID NO: 256)-A (herein referred to as BCY18520); A-(SEQ ID NO: 257)-A (herein referred to as BCY16672); A-(SEQ ID NO: 258)-A (herein referred to as BCY16673); A-(SEQ ID NO: 258)-A-[Sar6]-[KFl] (herein referred to as BCY16649); A-(SEQ ID NO: 258)-A-[K(PYA)] (herein referred to as BCY17237); Ac-A-(SEQ ID NO: 258)-A (herein referred to as BCY19585); and A-(SEQ ID NO: 259)-A (herein referred to as BCY16674); or a modified derivative and / or pharmaceutically acceptable salt thereof, or wherein the molecular scaffold is a tri-substituted 2,4,6-tris(bromomethyl)-s-triazine derivative of TBMT having the following structure: wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of X41-X42-X43-X44-X45-X46-X47-X48-X49-C-X50-X51-X52-X53-X54(SEQ ID NO: 6) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 260)-A (herein referred to as BCY17002); A-(SEQ ID NO: 260)-A-[K(PYA)] (herein referred to as BCY19745); A-(SEQ ID NO: 261)-A (herein referred to as BCY18130); A-(SEQ ID NO: 261)-A-[K(PYA)] (herein referred to as BCY20847); [PYA]-A-(SEQ ID NO: 261)-A (herein referred to as BCY20852); Ac-(SEQ ID NO: 261) (herein referred to as BCY21616); A-(SEQ ID NO: 261) (herein referred to as BCY21617); Ac-A-(SEQ ID NO: 261) (herein referred to as BCY21618); [PYA]-(SEQ ID NO: 261) (herein referred to as BCY21619); [GuanAc]-(SEQ ID NO: 261)-A (herein referred to as BCY23043); A-(SEQ ID NO: 261)-[CF3Ala] (herein referred to as BCY23080); A-(SEQ ID NO: 261)-S (herein referred to as BCY23081); A-(SEQ ID NO: 262)-A (herein referred to as BCY20848); A-(SEQ ID NO: 263)-A (herein referred to as BCY20849); A-(SEQ ID NO: 264)-A (herein referred to as BCY20850); A-(SEQ ID NO: 265)-A (herein referred to as BCY20851); A-(SEQ ID NO: 266)-A (herein referred to as BCY20853); A-(SEQ ID NO: 266) (herein referred to as BCY21620); A-(SEQ ID NO: 267)-A (herein referred to as BCY21622); A-(SEQ ID NO: 267)-A-[K(PYA)] (herein referred to as BCY21607); Ac-(SEQ ID NO: 268) (herein referred to as BCY21624); A-(SEQ ID NO: 268) (herein referred to as BCY21625); [PYA]-(SEQ ID NO: 268) (herein referred to as BCY21626); A-(SEQ ID NO: 269) (herein referred to as BCY21627); Ac-(SEQ ID NO: 270) (herein referred to as BCY22879); Ac-(SEQ ID NO: 271) (herein referred to as BCY22880); A-(SEQ ID NO: 272)-A (herein referred to as BCY23044); A-(SEQ ID NO: 273)-A (herein referred to as BCY23045); A-(SEQ ID NO: 274)-A (herein referred to as BCY23046); A-(SEQ ID NO: 275)-A (herein referred to as BCY23047); A-(SEQ ID NO: 276)-A (herein referred to as BCY23050); A-(SEQ ID NO: 277)-A (herein referred to as BCY23051); A-(SEQ ID NO: 278)-A (herein referred to as BCY23052); A-(SEQ ID NO: 279)-A (herein referred to as BCY23053); A-(SEQ ID NO: 280)-A (herein referred to as BCY23054); A-(SEQ ID NO: 281)-A (herein referred to as BCY23058); A-(SEQ ID NO: 282)-A (herein referred to as BCY23059); A-(SEQ ID NO: 283)-A (herein referred to as BCY23062); A-(SEQ ID NO: 284)-A (herein referred to as BCY23063); A-(SEQ ID NO: 285)-A (herein referred to as BCY23064); A-(SEQ ID NO: 286)-A (herein referred to as BCY23066); A-(SEQ ID NO: 287)-A (herein referred to as BCY23067); A-(SEQ ID NO: 288)-A (herein referred to as BCY23068); A-(SEQ ID NO: 289)-A (herein referred to as BCY23071); A-(SEQ ID NO: 290)-A (herein referred to as BCY23072); A-(SEQ ID NO: 291)-A (herein referred to as BCY23073); A-(SEQ ID NO: 292)-A (herein referred to as BCY23074); A-(SEQ ID NO: 293)-A (herein referred to as BCY23075); A-(SEQ ID NO: 294)-A (herein referred to as BCY23079); [GuanAc]-(SEQ ID NO: 295)-COOH (herein referred to as BCY27058); [GuanAc]-(SEQ ID NO: 295) (herein referred to as BCY27059); [CIA]-[K(PYA)]-(SEQ ID NO: 295)-A (herein referred to as BCY27064); [CIA]-[dK(PYA)]-(SEQ ID NO: 295)-A (herein referred to as BCY27065); [GuanAc]-(SEQ ID NO: 296) (herein referred to as BCY27060); [GuanAc]-(SEQ ID NO: 297) (herein referred to as BCY27061); [GuanAc]-(SEQ ID NO: 298) (herein referred to as BCY27062); [GuanAc]-(SEQ ID NO: 299) (herein referred to as BCY27063); [GuanAc]-(SEQ ID NO: 300) (herein referred to as BCY27066); [GuanAc]-(SEQ ID NO: 301) (herein referred to as BCY27067); [GuanAc]-(SEQ ID NO: 302) (herein referred to as BCY27068); A-(SEQ ID NO: 303)-A (herein referred to as BCY18131); A-(SEQ ID NO: 304)-A (herein referred to as BCY18132); A-(SEQ ID NO: 305)-A-[K(PYA)] (herein referred to as BCY19588); A-(SEQ ID NO: 306)-A (herein referred to as BCY19933); A-(SEQ ID NO: 307)-A (herein referred to as BCY19934); A-(SEQ ID NO: 308)-A (herein referred to as BCY19935); A-(SEQ ID NO: 309)-A (herein referred to as BCY19936); A-(SEQ ID NO: 309)-A-[K(PYA)] (herein referred to as BCY21606); Ac-(SEQ ID NO: 309) (herein referred to as BCY23139); Ac-A-(SEQ ID NO: 309)-A (herein referred to as BCY23140); [dA]-(SEQ ID NO: 309)-A (herein referred to as BCY32061); A-(SEQ ID NO: 309) (herein referred to as BCY32074); Ac-A-(SEQ ID NO: 309) (herein referred to as BCY32075); (SEQ ID NO: 309)-A (herein referred to as BCY32076); Ac-(SEQ ID NO: 309)-A (herein referred to as BCY32077); A-(SEQ ID NO: 309)-A-[dK(PYA)] (herein referred to as BCY32126); A-(SEQ ID NO: 309)-[K(PYA)] (herein referred to as BCY32127); A-(SEQ ID NO: 309)-[dK(PYA)] (herein referred to as BCY32128); A-(SEQ ID NO: 310)-A (herein referred to as BCY23138); A-(SEQ ID NO: 310)-A-[K(PYA)] (herein referred to as BCY24613); A-(SEQ ID NO: 311)-A (herein referred to as BCY32062); A-(SEQ ID NO: 312)-A (herein referred to as BCY32065); A-(SEQ ID NO: 313)-A (herein referred to as BCY32066); A-(SEQ ID NO: 314)-A (herein referred to as BCY32069); A-(SEQ ID NO: 315)-A (herein referred to as BCY32071); A-(SEQ ID NO: 316)-A (herein referred to as BCY32072); A-(SEQ ID NO: 317)-A (herein referred to as BCY32078); A-(SEQ ID NO: 318)-A (herein referred to as BCY32079); A-(SEQ ID NO: 319)-A (herein referred to as BCY32080); A-(SEQ ID NO: 320)-A (herein referred to as BCY32081); A-(SEQ ID NO: 321)-A (herein referred to as BCY32082); A-(SEQ ID NO: 322)-A (herein referred to as BCY32083); A-(SEQ ID NO: 323)-A (herein referred to as BCY32084); A-(SEQ ID NO: 324)-A (herein referred to as BCY32085); A-(SEQ ID NO: 325)-A (herein referred to as BCY32086); A-(SEQ ID NO: 326)-A (herein referred to as BCY32087); A-(SEQ ID NO: 327)-A (herein referred to as BCY32088); A-(SEQ ID NO: 328)-A (herein referred to as BCY32089); A-(SEQ ID NO: 329)-A (herein referred to as BCY32090); A-(SEQ ID NO: 330)-A (herein referred to as BCY32091); A-(SEQ ID NO: 331)-A (herein referred to as BCY32092); A-(SEQ ID NO: 332)-A (herein referred to as BCY32093); A-(SEQ ID NO: 333)-A (herein referred to as BCY32095); A-(SEQ ID NO: 334)-A (herein referred to as BCY32096); A-(SEQ ID NO: 335)-A (herein referred to as BCY32098); A-(SEQ ID NO: 336)-A (herein referred to as BCY32099); A-(SEQ ID NO: 337)-A (herein referred to as BCY32100); A-(SEQ ID NO: 338)-A (herein referred to as BCY32101); A-(SEQ ID NO: 339)-A (herein referred to as BCY32103); A-(SEQ ID NO: 340)-A (herein referred to as BCY32104); A-(SEQ ID NO: 341)-A (herein referred to as BCY32105); A-(SEQ ID NO: 342)-A (herein referred to as BCY32106); A-(SEQ ID NO: 343)-A (herein referred to as BCY32107); A-(SEQ ID NO: 344)-A (herein referred to as BCY32108); A-(SEQ ID NO: 345)-A (herein referred to as BCY32109); A-(SEQ ID NO: 346)-A (herein referred to as BCY32110); A-(SEQ ID NO: 347)-A (herein referred to as BCY32112); A-(SEQ ID NO: 348)-A (herein referred to as BCY32113); A-(SEQ ID NO: 349)-A (herein referred to as BCY32114); A-(SEQ ID NO: 350)-A (herein referred to as BCY32115); A-(SEQ ID NO: 351)-A (herein referred to as BCY32116); A-(SEQ ID NO: 352)-A (herein referred to as BCY32117); A-(SEQ ID NO: 353)-A (herein referred to as BCY32120); A-(SEQ ID NO: 354)-A (herein referred to as BCY32121); A-(SEQ ID NO: 355)-A (herein referred to as BCY32122); A-(SEQ ID NO: 356)-A (herein referred to as BCY32123); A-(SEQ ID NO: 357)-A (herein referred to as BCY32124); A-(SEQ ID NO: 358)-A (herein referred to as BCY32125); A-(SEQ ID NO: 359)-A (herein referred to as BCY19937); A-(SEQ ID NO: 360)-A (herein referred to as BCY19938); A-(SEQ ID NO: 361)-A (herein referred to as BCY19939); A-(SEQ ID NO: 362)-A (herein referred to as BCY19940); A-(SEQ ID NO: 363)-A (herein referred to as BCY19941); A-(SEQ ID NO: 364)-A (herein referred to as BCY19942); A-(SEQ ID NO: 365)-A (herein referred to as BCY19943); and A-(SEQ ID NO: 366)-A (herein referred to as BCY18253); or a modified derivative and / or pharmaceutically acceptable salt thereof. 9. A multimeric binding complex which comprises at least two bicyclic peptide ligands according to any one of aspects 2 to 8, wherein said peptide ligands may be the same or different. 10. The multimeric binding complex according to aspect 9 which comprises more than one bicyclic peptide which are the same (i.e. homomultimers). 11. The multimeric binding complex according to aspect 9 which comprises bicyclic peptides which are different (i.e. heteromultimers). 12. The multimeric binding complex according to aspect 9 which comprises two bicyclic peptides which are either the same (i.e. homodimers) or different (i.e. heterodimers), such as: BCY16282 AF488-AHDA-(amido-Peg10-triazolyl)[BCY15751]2 BCY26427 GTA-[amido-Peg10-triazolyl]2[BCY25826]2 BCY26435 GTA-[amido-Peg10-triazolyl]2[BCY24613]2 BCY28218 N-(Biotin-PEG23]-N-bis(PEG3-azide)[BCY24613]2 BCY28219 N-(Biotin-PEG23]-N-bis(PEG3-azide)[BCY21996]2 BCY28220 N-(Biotin-PEG23]-N-bis(PEG3-azide)[BCY25826]2 BCY28885 N-(Biotin-PEG23]-N-bis(PEG3-azide)[BCYBCY19741]2 BCY28887 N-(Biotin-PEG23]-N-bis(PEG3-azide)[BCY19743]2 BCY28222 N-(Biotin-PEG10)-N-bis(PEG10-azide)[BCY23767]2 BCY28223 N-(Biotin-PEG10)-N-bis(PEG10-azide)[BCY24613]2 BCY28224 N-(Biotin-PEG10)-N-bis(PEG10-azide)[BCY21996]2 BCY28225 N-(Biotin-PEG10)-N-bis(PEG10-azide)[BCY25826]2 BCY28886 N-(Biotin-PEG10)-N-bis(PEG10-azide)[BCY19741]2 BCY28888 N-(Biotin-PEG10)-N-bis(PEG10-azide)[BCY19743]2 BCY26436 GTA-[amido-Peg23-triazolyl]2[BCY24613]2 BCY31478 N-(amine-PEG10)-[BDP558-N3SC2]-N-bis(PEG10-azide)[BCY24613]2 BCY34406 N-(acid-PEG10)-[BDP558-N3SC1]-N-bis(PEG10-azide)[BCY24613]2 13. The multimeric binding complex according to aspect 9 which comprises three bicyclic peptides which are either the same (i.e. homotrimers) or different (i.e. heterotrimers), such as wherein the heterotrimer comprises one bicyclic peptide of a first sequence and two bicyclic peptides of a second sequence, in particular: BCY25832 TCA-[amido-Peg10-triazolyl]3[BCY25826]3 BCY26437 TCA-[amido-Peg10-triazolyl]3[BCY24613]3 BCY28283 TCA-[amido-Peg5-triazolyl]3[BCY20840]3 BCY26442 TCA-[amido-Peg23-triazolyl]3[BCY24613]3 14. The multimeric binding complex according to aspect 9 which comprises four bicyclic peptides which are either the same (i.e. homotetramers) or different (i.e. heterotetramers), such as wherein the heterotetramer comprises one bicyclic peptide of a first sequence and three bicyclic peptides of a second sequence, or wherein the heterotetramer comprises two bicyclic peptides of a first sequence and two bicyclic peptides of a second sequence, in particular: BCY15926 TET-[amido-Peg23-triazolyl]4[BCY15751]4 BCY25831 TET-[amido-Peg10-triazolyl]4[BCY25826]4 BCY26438 TET-[amido-Peg5-triazolyl]4[BCY24613]4 BCY26439 TET-[amido-Peg10-triazolyl]4[BCY24613]4 BCY21835 TET-[amido-Peg23-triazolyl]4[BCY20840]4 BCY21481 TET-[amido-Peg23-triazolyl]4[BCY19177]4 BCY21483 TET-[amido-Peg23-triazolyl]4[BCY21040]4 BCY29425 TET-[amido-Peg5-triazolyl]4[BCY23706]4 BCY29427 TET-[amido-Peg23-triazolyl]4[BCY23706]4 BCY28229 TET-[amido-Peg5-triazolyl]4[BCY21996]4 BCY28230 TET-[amido-Peg10-triazolyl]4[BCY21996]4 BCY26433 TET-[amido-Peg10-triazolyl]4[BCY23767]4 BCY26432 TET-[amido-Peg5-triazolyl]4[BCY23767]4 BCY28884 TET-[amido-Peg5-triazolyl]4[BCY19743]4 BCY30493 TET-[amido-Peg5-triazolyl]4[BCY28840]4 BCY30494 TET-[amido-Peg10-triazolyl]4[BCY28840]4 BCY30502 TET-[amido-Peg5-triazolyl]4[BCY28841]4 BCY30503 TET-[amido-Peg10-triazolyl]4[BCY28841]4 BCY30504 TET-[amido-Peg23-triazolyl]4[BCY28841]4 BCY26428 TET-[amido-Peg5-triazolyl]4[BCY25826]4 BCY25828 TET-[amido-Peg23-triazolyl]4[BCY25826]4 BCY26440 TET-[amido-Peg23-triazolyl]4[BCY24613]4 BCY26434 TET-[amido-Peg23-triazolyl]4[BCY23767]4 BCY29426 TET-[amido-Peg10-triazolyl]4[BCY23706]4 BCY28883 TET-[amido-Peg5-triazolyl]4[BCY19741]4 15. A pharmaceutical composition which comprises the peptide ligand according to aspect 1, or bicyclic peptide ligand according to any one of aspects 2 to 8, or multimeric binding complex according to any one of aspects 9 to 14, in combination with one or more pharmaceutically acceptable excipients. 16. The peptide ligand according to aspect 1, or bicyclic peptide ligand according to any one of aspects 2 to 8, or multimeric binding complex according to any one of aspects 9 to 14, or pharmaceutical composition according to aspect 15, for use in for use in preventing, suppressing or treating a disease or disorder mediated by TLR3. 5

Claims

CLAIMS 1. A peptide ligand, comprising a polypeptide having an amino acid sequence selected from: C-X1-X2-X3-C-X4-X5-X6-X7-X8-X9-C (SEQ ID NO: 1); C-X10-X11-Y-Y-C-X12-Q-T-X13-X14-F-C (SEQ ID NO: 2); X15-X16-X17-X18-X19-X20-X21-X22-X23-X24-X25-X26-X27-X28-X29(SEQ ID NO: 3); C-Q-P-T-X30-X31-C-X32-X33-X34-X35-X36-X37-C (SEQ ID NO: 4); C-Y-Y-X38-X39-X40-Y-A-C-L-D-C (SEQ ID NO: 5); and X41-X42-X43-X44-X45-X46-X47-X48-X49-C-X50-X51-X52-X53-X54(SEQ ID NO: 6); wherein: X1represents D, N, P, Y, 26DiMeTyr, 2FTyr, 3FTyr, or 4FPhe; X2 represents A, I, N, P, S, T, Aze, Cba, Cis-HyP, tBuAla, or tBuGly; X3represents A, G, N, P, Q, R, Aib, Aze, Cis-HyP, dA, HyP, or Pip; X4represents L, S, or Cba; X5represents K, P, R, W, 5FTrp, 5MeOTrp, 6ClTrp, 6FTrp, 6MeTrp, Agb, HArg, Trp(Me), or Trp(S); X6represents M, R, or HArg; X7represents A, F, Q, Y, 2FTyr, 3FTyr, 3tBuTyr, or 4FPhe; X8represents H, I, N, V, Cbg, His1Me, His3Me, or tBuGly; X9represents D, F, L, 1Nal, 2Nal, 4tBuPhe, Cba, or tBuAla; X10represents S or T; X11represents K or S; X12represents E or Q; X13represents R or V; X14represents H or R; X15represents C or dC; X16represents A, D, H, I, L, M, N, P, S, T, W, CF3Nva, dP, HyP, Nle, Nva, or TfNle; X17represents E, L, N, P, Q, S, T, Y, 26DiMeTyr, Cba, dL, or tBuAla; X18represents D, E, L, P, R, T, Agb, Cba, Cit, dD, HArg, or tBuAla; X19represents A, E, I, L, M, Q, V, AlloIle, Cba, CF3Ala, dL, HLeu, Nle, or tBuAla; X20represents C or dC; X21represents A, E, F, L, Q, R, T, W, Y, 1Nal, 2FPhe, 2MePhe, 2Nal, 3FPhe, 3MePhe, 4FPhe, 4MePhe, or dE; X22represents A, R, V, Y, 26DiMeTyr, 2FTyr, 3FTyr, 3tBuTyr, 4FPhe, DOPA, or dY; X23represents A, D, W, 1Nal, 2Nal, 4MeoTrp, 5FTrp, dW, Gla, or Trp(S); X24represents A, D, E, H, M, Q, S, Y, dS, K(PYA), or Nle;X25represents E, F, L, N, S, T, V, Cba, or dS; X26represents R, W, Y, 1Nal, 2FTyr, 2MeTrp, 2Nal, 3FTyr, 4FTrp, 5FTrp, 5MeTrp, 6FTrp, 6MeTrp, 7FTrp, 7MeTrp, Cit, dR, HArg, or Trp(Me); X27represents G, R, S, Agb, Cit, dA, dE, or HArg; X28represents L, P, 44DFP, 4FlPro, Aze, Cba, dL, HyP, Pip, tBuAla, or trans-4FlPro; X29represents C, dC, or Cysam; X30represents P, Cis-HyP, HyP, or Pip; X31represents E, Q, or R; X32represents P, Aze, Cis-HyP, or HyP; X33represents F, Y, 2FTyr, 2Nal, 3FTyr, 4FPhe, or 4tBuPhe; X34represents N, S, or Dap; X35represents T or Dap; X36represents W, 1Nal, 2Nal, 4MeoTrp, 5FTrp, 5MeoTrp, 6ClTrp, 6FTrp, AzaTrp, or Trp(S); X37represents P, Aze, Cis-HyP, HyP, or Pip; X38represents E or P; X39represents D or N; X40represents W or Y; X41represents C or dC; X42represents A, D, E, G, K, N, P, S, T, V, Y, 3HyV, Aib, CF3Ala, dA, Dap, dK(PYA), dS, HSer, or K(PYA); X43represents N, T, or 3HyV; X44represents D, E, P, 4FlPro, Cis-Hyp, HyP, or trans-4FlPro; X45represents A, H, M, Q, S, V, Y, 1Nal, 26DiMeTyr, 2FTyr, 2Nal, 3FTyr, 4FPhe, DOPA, or HSer; X46represents A, E, F, I, M, V, 2FPhe, 4CF3Phe, Cba, CF3Nva, Nle, Nva, tBuAla, or TfNle; X47represents A, E, S, T, W, 1Nal, 2MeTrp, 4FTrp, 4MeTrp, 5FTrp, 5MeTrp, 6FTrp, 6MeTrp, 7FTrp, 7MeTrp, AzaTrp, CF3Ala, or Dap; X48represents K, R, Y, 2FTyr, 3FTyr, Agb, DOPA, HArg, or Orn; X49represents A, D, L, V, W, 1Nal, 2Nal, 3HyV, 4FTrp, 5FTrp, 5MeoTrp, 6FTrp, AzaTrp, C5g, Cbg, tBuGly, or Trp(S); X50represents E, M, Q, R, S, T, Arg(Me), Dap, HArg, or PG; X51represents A, E, K, M, R, S, T, 3HyV, Cit, HArg, or Orn; X52represents A, G, L, M, N, P, Q, Cba, dA, dK(PYA), K(PYA), Nle, Nva, R- aMeLys(PYA), S-aMeLys(PYA), or tBuAla;X53represents D, I, L, M, V, EPA, Nle, Nva, or tBuGly; and / or X54represents C, dC, or Cysam; or a modified derivative and / or pharmaceutically acceptable salt thereof.

2. A bicyclic peptide ligand capable of binding TLR3, or a pharmaceutically acceptable salt thereof, which comprises a peptide ligand comprising a polypeptide comprising three reactive groups, wherein the polypeptide is attached to a molecular scaffold.

3. A bicyclic peptide ligand according to claim 2, or a pharmaceutically acceptable salt thereof, wherein the peptide ligand is as defined in claim 1, and wherein the three cysteine or Cysam residues of said peptide ligand form covalent bonds with the molecular scaffold to form two loop sequences.

4. The bicyclic peptide ligand according to claim 3, wherein the peptide ligand of C-X1-X2-X3- C-X4-X5-X6-X7-X8-X9-C (SEQ ID NO: 1) comprises a polypeptide having an amino acid sequence selected from: CDI ACLKM YNFC (SEQ ID NO: 7); CDI GCLR MYNFC (SEQ ID NO: 8); CD[tBuAla]G CLRMY NFC (SEQ ID NO: 9); CD[tBuGly]G CLRMY NFC (SEQ ID NO: 10); CD[Cba]G CLRM YNFC (SEQ ID NO: 11); CDI [dA]CLRM YNFC (SEQ ID NO: 12); CDI [Aib]CLR MYNFC (SEQ ID NO: 13); CDI GC[Cba]R MYNFC (SEQ ID NO: 14): CDI GCL[HArg]M YNFC (SEQ ID NO: 15): CDI GCL[Agb]M YNFC (SEQ ID NO: 16); CDI GCLR MYN[1Nal] C (SEQ ID NO: 17); CDI GCLR MYN[2Nal] C (SEQ ID NO: 18); CDI GCLR MYN[4tBuPhe]C (SEQ ID NO: 19); CDI QCLR MYNFC (SEQ ID NO: 20); CNI QCLR MYNFC (SEQ ID NO: 21); CDI RCLRM YNFC (SEQ ID NO: 22); CDI NCLRM YNFC (SEQ ID NO: 23); CPPG CSPRFH LC (SEQ ID NO: 24); CPPG CSPRY HLC (SEQ ID NO: 25; herein referred to as BCY21542 when complexed with a derivative of TATB which has the following structure:wherein * denotes the point of attachment of the three cysteine residues); CP[Cis-HyP]G CSPRY HLC (SEQ ID NO: 26); CP[Aze]G CSPRYH LC (SEQ ID NO: 27); CPPG CSP[HArg]YHLC (SEQ ID NO: 28); CPPG CSPR[4FPhe]H LC (SEQ ID NO: 29); CPPG CSPR[3tBuTyr]H LC (SEQ ID NO: 30): CPPG CSPR[3FTyr] HLC (SEQ ID NO: 31); CPPG CSPR[2FTyr] HLC (SEQ ID NO: 32); CPPG CSPRY [His1Me]LC (SEQ ID NO: 33); CPPG CSPRY [His3Me]LC (SEQ ID NO: 34); CPPG CSPRY H[tBuAla]C (SEQ ID NO: 35); CPPG CSPRY H[Cba]C (SEQ ID NO: 36); CPPG CSPRY NLC (SEQ ID NO: 37); CYN PCLWR QVDC (SEQ ID NO: 38; herein referred to as BCY21497 when complexed with a tri-substituted 2,4,6-tris(bromomethyl)-s-triazine derivative of TBMT having the following structure:wherein * denotes the point of attachment of the three cysteine residues); CYAP CLWR QVDC (SEQ ID NO: 39); CYN PCLWR AVDC (SEQ ID NO: 40); C[4FPhe]NP CLWRQ VDC (SEQ ID NO: 41); C[26DiMeTyr]N PCLWR QVDC (SEQ ID NO: 42); C[3FTyr]N PCLWRQVDC (SEQ ID NO: 43); C[2FTyr]N PCLWRQVDC (SEQ ID NO: 44);CYN [HyP]CLWR QVDC (SEQ ID NO: 45); CYN [Cis-HyP]CLWRQ VDC (SEQ ID NO: 46); CYN [Aze]C LWRQ VDC (SEQ ID NO: 47); CYN [Pip]CLWRQVD C (SEQ ID NO: 48); CYN PC[Cba]WRQVDC (SEQ ID NO: 49); CYN PCL[6MeTrp]RQVDC (SEQ ID NO: 50); CYN PCL[6FTrp]RQ VDC (SEQ ID NO: 51); CYN PCL[5FTrp]RQ VDC (SEQ ID NO: 52); CYN PCL[6ClTrp]RQV DC (SEQ ID NO: 53); CYN PCL[5MeoTrp]RQVDC (SEQ ID NO: 54); CYN PCL[Trp(S)]RQVDC (SEQ ID NO: 55); CYN PCL[Trp(Me)]RQVD C (SEQ ID NO: 56); CYN PCLWR Q[tBuGly]DC (SEQ ID NO: 57); CYN PCLWR Q[Cbg]DC (SEQ ID NO: 58); CYN PCLWR QID C (SEQ ID NO: 59); CYSP CLWR QVDC (SEQ ID NO: 60); and CYTPC LWRQ VDC (SEQ ID NO: 61), such as: wherein the molecular scaffold is a derivative of TATA which has the following structure:wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of C-X1-X2-X3-C-X4-X5-X6-X7-X8-X9-C (SEQ ID NO: 1) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 7)-A-[Sar6]-[KFl] (herein referred to as BCY15200); A-(SEQ ID NO: 7)-A (herein referred to as BCY15212); A-(SEQ ID NO: 8)-A (herein referred to as BCY15747); A-(SEQ ID NO: 8)-A-[K(PYA)] (herein referred to as BCY19281); A-(SEQ ID NO: 9)-A (herein referred to as BCY17064); A-(SEQ ID NO: 10)-A (herein referred to as BCY17065); A-(SEQ ID NO: 11)-A (herein referred to as BCY17066);A-(SEQ ID NO: 12)-A (herein referred to as BCY17067); A-(SEQ ID NO: 13)-A (herein referred to as BCY17068); A-(SEQ ID NO: 14)-A (herein referred to as BCY17070); A-(SEQ ID NO: 15)-A (herein referred to as BCY17071); A-(SEQ ID NO: 16)-A (herein referred to as BCY17072); A-(SEQ ID NO: 17)-A (herein referred to as BCY17079); A-(SEQ ID NO: 18)-A (herein referred to as BCY17080); A-(SEQ ID NO: 19)-A (herein referred to as BCY17081); A-(SEQ ID NO: 20)-A (herein referred to as BCY16675); A-(SEQ ID NO: 21)-A (herein referred to as BCY16676); A-(SEQ ID NO: 22)-A (herein referred to as BCY16677); and A-(SEQ ID NO: 23)-A (herein referred to as BCY16678); or a modified derivative and / or pharmaceutically acceptable salt thereof, or wherein the molecular scaffold is a derivative of TATB which has the following structure:wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of C-X1-X2-X3-C-X4-X5-X6-X7-X8-X9-C (SEQ ID NO: 1) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 24)-A (herein referred to as BCY16997); A-(SEQ ID NO: 25)-A (herein referred to as BCY18125); A-(SEQ ID NO: 25)-A-[K(PYA)] (herein referred to as BCY19741); A-(SEQ ID NO: 25) (herein referred to as BCY21538); Ac-A-(SEQ ID NO: 25) (herein referred to as BCY21539); (SEQ ID NO: 25)-A (herein referred to as BCY21540); Ac-(SEQ ID NO: 25)-A (herein referred to as BCY21541); Ac-(SEQ ID NO: 25) (herein referred to as BCY21543); Ac-A-(SEQ ID NO: 25)-A (herein referred to as BCY21544); A-(SEQ ID NO: 25)-DKTTV (herein referred to as BCY21769); TVKTP-(SEQ ID NO: 25)-A (herein referred to as BCY21775);A-(SEQ ID NO: 25)-DIHNN (herein referred to as BCY21777); A-(SEQ ID NO: 26)-A (herein referred to as BCY21550); A-(SEQ ID NO: 27)-A (herein referred to as BCY21551); A-(SEQ ID NO: 28)-A (herein referred to as BCY21558); A-(SEQ ID NO: 29)-A (herein referred to as BCY21561); A-(SEQ ID NO: 30)-A (herein referred to as BCY21562); A-(SEQ ID NO: 31)-A (herein referred to as BCY21564); A-(SEQ ID NO: 32)-A (herein referred to as BCY21565); A-(SEQ ID NO: 33)-A (herein referred to as BCY21566); A-(SEQ ID NO: 34)-A (herein referred to as BCY21567); A-(SEQ ID NO: 35)-A (herein referred to as BCY21568); A-(SEQ ID NO: 36)-A (herein referred to as BCY21569); and A-(SEQ ID NO: 37)-A (herein referred to as BCY16998); or a modified derivative and / or pharmaceutically acceptable salt thereof, or wherein the molecular scaffold is a tri-substituted 2,4,6-tris(bromomethyl)-s-triazine derivative of TBMT, or TCTZ, having the following structure:wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of C-X1-X2-X3-C-X4-X5-X6-X7-X8-X9-C (SEQ ID NO: 1) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 38)-A (herein referred to as BCY18251); A-(SEQ ID NO: 38)-A-[K(PYA)] (herein referred to as BCY19587); A-(SEQ ID NO: 38) (herein referred to as BCY21493); (SEQ ID NO: 38)-A (herein referred to as BCY21495); Ac-(SEQ ID NO: 38) (herein referred to as BCY21498); YYYE W-(SEQ ID NO: 38)-A (herein referred to as BCY21773); A-(SEQ ID NO: 39)-A (herein referred to as BCY21485); A-(SEQ ID NO: 40)-A (herein referred to as BCY21490); A-(SEQ ID NO: 41)-A (herein referred to as BCY21500); A-(SEQ ID NO: 42)-A (herein referred to as BCY21502);A-(SEQ ID NO: 43)-A (herein referred to as BCY21503); A-(SEQ ID NO: 44)-A (herein referred to as BCY21504); A-(SEQ ID NO: 45)-A (herein referred to as BCY21505); A-(SEQ ID NO: 46)-A (herein referred to as BCY21506); A-(SEQ ID NO: 47)-A (herein referred to as BCY21507); A-(SEQ ID NO: 48)-A (herein referred to as BCY21508); A-(SEQ ID NO: 49)-A (herein referred to as BCY21510); A-(SEQ ID NO: 50)-A (herein referred to as BCY21515); A-(SEQ ID NO: 51)-A (herein referred to as BCY21517); A-(SEQ ID NO: 52)-A (herein referred to as BCY21518); A-(SEQ ID NO: 53)-A (herein referred to as BCY21519); A-(SEQ ID NO: 54)-A (herein referred to as BCY21521); A-(SEQ ID NO: 55)-A (herein referred to as BCY21522); A-(SEQ ID NO: 56)-A (herein referred to as BCY21523); A-(SEQ ID NO: 57)-A (herein referred to as BCY21527); A-(SEQ ID NO: 58)-A (herein referred to as BCY21528); A-(SEQ ID NO: 59)-A (herein referred to as BCY19930); A-(SEQ ID NO: 59)-VYNVN (herein referred to as BCY21776 ); A-(SEQ ID NO: 60)-A (herein referred to as BCY19931); and A-(SEQ ID NO: 61)-A (herein referred to as BCY19932); or a modified derivative and / or pharmaceutically acceptable salt thereof.

5. The bicyclic peptide ligand according to claim 3, wherein the peptide ligand of C-X10-X11-Y- Y-C-X12-Q-T-X13-X14-F-C (SEQ ID NO: 2) comprises an amino acid sequence selected from: CTSYY CEQTRH FC (SEQ ID NO: 62); CTKYY CEQTRH FC (SEQ ID NO: 63); and CSKY YCQQ TVRFC (SEQ ID NO: 64), such as: wherein the molecular scaffold is a tri-substituted 2,4,6-tris(bromomethyl)-s-triazine derivative of TBMT, or TCTZ, having the following structure:wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of C-X10-X11-Y-Y-C-X12-Q-T-X13-X14-F-C (SEQ ID NO: 2) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 62)-A (herein referred to as BCY17006); A-(SEQ ID NO: 63)-A (herein referred to as BCY18134); A-(SEQ ID NO: 63)-A-[K(PYA] (herein referred to as BCY19746); and A-(SEQ ID NO: 64)-A (herein referred to as BCY17012); or a modified derivative and / or pharmaceutically acceptable salt thereof.

6. The bicyclic peptide ligand according to claim 3, wherein the peptide ligand of X15-X16-X17- X18-X19-X20-X21-X22-X23-X24-X25-X26-X27-X28-X29(SEQ ID NO: 3) comprises an amino acid sequence selected from: CTNE VCTYWYNRGLC (SEQ ID NO: 65); CAN EVCEYWYNRG LC (SEQ ID NO: 66); CPLD LCEYWSFRGLC (SEQ ID NO: 67); CTNE VCRYWYNRG LC (SEQ ID NO: 68); CDS PVCEYWSFRGLC (SEQ ID NO: 69); CHN EVCEYWSFRG LC (SEQ ID NO: 70); CSN EVCEYWSFRGLC (SEQ ID NO: 71); CSN PVCEYWSFRGLC (SEQ ID NO: 72); CNN PVCEYWSFRG LC (SEQ ID NO: 73); CDN EVCEYWSFRG LC (SEQ ID NO: 74); CTSEV CEYWSFRGLC (SEQ ID NO: 75); CSTLVC QRDQ LYSLC (SEQ ID NO: 76); CHN EVCLYWYNRG LC (SEQ ID NO: 77); CWNPVCE YWYN RGLC (SEQ ID NO: 78); CATLQ CQRD MLYGLC (SEQ ID NO: 79); CSTLVC QRDQ LYGLC (SEQ ID NO: 80); CST[tBuAla]VC QRDQ LYGLC (SEQ ID NO: 81); CST[Cba]V CQRDQ LYGLC (SEQ ID NO: 82); CSTL[tBuAla]C QRDQ LYGLC (SEQ ID NO: 83); CSTLVC QRD[Nle] LYGLC (SEQ ID NO: 84); CSTLVC QRDQ [Cba]YGLC (SEQ ID NO: 85); CSTLVC QRDQ LY[dA]LC (SEQ ID NO: 86); CSTLVC QRDQ LYG[tBuAla]C (SEQ ID NO: 87); CSTLVC QRDQ LYG[Cba]C (SEQ ID NO: 88);CST[tBuAla]VC QRDQ LY[dA]LC (SEQ ID NO: 89); CNP LICQ RDQLYG LC (SEQ ID NO: 90); CI SLACQR DQLYG LC (SEQ ID NO: 91); CSTLEC QRDQ LYGLC (SEQ ID NO: 92); CNTLV CQRDQ LYGLC (SEQ ID NO: 93); CTQLM CQR DQLYGLC (SEQ ID NO: 94); CTELM CQRD QLYGLC (SEQ ID NO: 95); CTE[tBuAla]M CQRD QLY[dA]LC (SEQ ID NO: 96); CTELM CQRD QLY[dA]LC (SEQ ID NO: 97); CTE[tBuAla]M CQRD QLYGLC (SEQ ID NO: 98); CTELAC QRDQ LYGLC (SEQ ID NO: 99); CTEL[Nle] CQR DQLYGLC (SEQ ID NO: 100); CTEL[HLeu]C QRDQ LYGLC (SEQ ID NO: 101); CTELM CQR[Gla]QLYG LC (SEQ ID NO: 102); CTELM CQRD QL[3FTyr]GLC (SEQ ID NO: 103); CTELM CQRD QL[2FTyr]GLC (SEQ ID NO: 104); CAN TVCAYWETRGLC (SEQ ID NO: 105); CAN TVCAY[5FTrp] ETRGLC (SEQ ID NO: 106); CPLD LCEYWSVRGLC (SEQ ID NO: 107); CPLD LCEYWSSRGLC (SEQ ID NO: 108); C[HyP]LDLC EYWS SRGLC (SEQ ID NO: 109); CP[tBuAla]D LCEYWSSRGLC (SEQ ID NO: 110); CP[Cba]D LCEYWSSRGLC (SEQ ID NO: 111); CPLD [AlloIle]CEY WSSR GLC (SEQ ID NO: 112); CPLD [tBuAla]CEYWSSRGLC (SEQ ID NO: 113); CPLD [Cba]CEYWSSRGLC (SEQ ID NO: 114); CPLD VCEYWSSRGLC (SEQ ID NO: 115); CPLD LCE[4FPhe]WS SRGLC (SEQ ID NO: 116); CPLD LCEY[2Nal]S SRGLC (SEQ ID NO: 117); CPLD LCEY[1Nal]S SRGLC (SEQ ID NO: 118); CPLD LCEY[5FTrp]S SRGLC (SEQ ID NO: 119); CPLD LCEY[4MeoTrp]SSRG LC (SEQ ID NO: 120); CPLD LCEY[Trp(S)]SSRGLC (SEQ ID NO: 121); CPLD LCEYWSS[HArg]GLC (SEQ ID NO: 122); CPLD LCEYWSS[Cit]GLC (SEQ ID NO: 123); CPLD LCEYWSSR[dA]LC (SEQ ID NO: 124);CPLD LCEYWSSRG[tBuAla]C (SEQ ID NO: 125); CPLD LCEYWSSRG[Cba]C (SEQ ID NO: 126); [dC][dP][dL][dD][dL][dC][dE][dY][dW] [dS][dS][dR]G[dL][dC] (SEQ ID NO: 127); CP[Cba]D LCEY[5FTrp] SSRGLC (SEQ ID NO: 128); CPLD LCEYW[K(PYA)]SRG LC (SEQ ID NO: 129, herein referred to as BCY21632 when complexed with a derivative of TATA which has the following structure:wherein * denotes the point of attachment of the three cysteine residues); CPLD LCEYW[K(PYA)]SRG L[Cysam] (SEQ ID NO: 130, herein referred to as BCY21637 when complexed with a derivative of TATA which has the following structure:wherein * denotes the point of attachment of the three cysteine residues); CPLD LCEY[5FTrp]E SRGLC (SEQ ID NO: 131); CPN DLCEY[5FTrp] SSRGLC (SEQ ID NO: 132); CPLD LCEY[5FTrp]S SR[dA]LC (SEQ ID NO: 133); CPLD LCEY[5FTrp]S SR[dE]LC (SEQ ID NO: 134); CPLD [tBuAla]CEY[5FTrp]S S[HArg][dA]LC (SEQ ID NO: 135); CP[Cba]D LCEY[5FTrp] SS[HArg][dA]LC (SEQ ID NO: 136); CPN DLCEYWSVRG LC (SEQ ID NO: 137); CI TLQCARD MLYGLC (SEQ ID NO: 138); CSTLQ CERDM LYGLC (SEQ ID NO: 139); CI SLACARD MLYGLC (SEQ ID NO: 140); CSTLQ CQRD MLYGLC (SEQ ID NO: 141); CM YRACWVAEEWRPC (SEQ ID NO: 142); CM YRACYY DHEWRPC (SEQ ID NO: 143);CM YRACFYD DEWR PC (SEQ ID NO: 144); CM YRACAY DDEWRPC (SEQ ID NO: 145); CM YRACFAD DEWR PC (SEQ ID NO: 146); CM YRACFYA DEWR PC (SEQ ID NO: 147); CM YRACFYD AEWR PC (SEQ ID NO: 148); C[Nle] YRACFY DDEWRPC (SEQ ID NO: 149); C[Nva]YRA CFYDDE WRPC (SEQ ID NO: 150); C[TfNle]YRA CFYDDE WRPC (SEQ ID NO: 151); C[CF3Nva]YR ACFYDD EWRP C (SEQ ID NO: 152); CM [26DiMeTyr]RACFYD DEWR PC (SEQ ID NO: 153); CM Y[HArg]A CFYDDE WRPC (SEQ ID NO: 154); CM Y[Agb]ACFYDD EWRP C (SEQ ID NO: 155); CM Y[Cit]ACFYDD EWRP C (SEQ ID NO: 156); CM YR[CF3Ala]CFYDDEWRPC (SEQ ID NO: 157); CM YRAC[1Nal] YDDEWRPC (SEQ ID NO: 158); CM YRAC[2Nal] YDDEWRPC (SEQ ID NO: 159); CM YRAC[4MePhe] YDDEWRPC (SEQ ID NO: 160); CM YRAC[3MePhe] YDDEWRPC (SEQ ID NO: 161); CM YRAC[2MePhe] YDDEWRPC (SEQ ID NO: 162); CM YRAC[4FPhe]YD DEWR PC (SEQ ID NO: 163); CM YRAC[3FPhe]YD DEWR PC (SEQ ID NO: 164); CM YRAC[2FPhe]YD DEWR PC (SEQ ID NO: 165); CM YRACF[4FPhe]DD EWR PC (SEQ ID NO: 166); CM YRACF[3tBuTyr]DD EWRP C (SEQ ID NO: 167); CM YRACF[26DiMeTyr]D DEWR PC (SEQ ID NO: 168); CM YRACF[3FTyr] DDEWRPC (SEQ ID NO: 169); CM YRACF[2FTyr] DDEWRPC (SEQ ID NO: 170); CM YRACF[DOPA]DDE WRPC (SEQ ID NO: 171); CM YRACFYD DE[1Nal]R PC (SEQ ID NO: 172); CM YRACFYD DE[2Nal]R PC (SEQ ID NO: 173); CM YRACFYD DE[4FTrp]R PC (SEQ ID NO: 174); CM YRACFYD DE[5FTrp]R PC (SEQ ID NO: 175); CM YRACFYD DE[6FTrp]R PC (SEQ ID NO: 176); CM YRACFYD DE[7FTrp]R PC (SEQ ID NO: 177); CM YRACFYD DE[Trp(Me)]RPC (SEQ ID NO: 178); CM YRACFYD DE[2MeTrp]RPC (SEQ ID NO: 179);CM YRACFYD DE[5MeTrp]RPC (SEQ ID NO: 180); CM YRACFYD DE[6MeTrp]RPC (SEQ ID NO: 181); CM YRACFYD DE[7MeTrp]RPC (SEQ ID NO: 182); CM YRACFYD DEW[HArg]PC (SEQ ID NO: 183); CM YRACFYD DEW[Agb]P C (SEQ ID NO: 184); CM YRACFYD DEW[Cit]P C (SEQ ID NO: 185); CM YRACFYD DEWR [HyP]C (SEQ ID NO: 186); CM YRACFYD DEWR [Aze]C (SEQ ID NO: 187); CM YRACFYD DEWR [Pip]C (SEQ ID NO: 188); CM YRACFYD DEWR [44DFP]C (SEQ ID NO: 189); CM YRACFYD DEWR [4FlPro]C (SEQ ID NO: 190); CM YRACFYD DEWR [trans-4FlPro]C (SEQ ID NO: 191); C[CF3Nva]YR ACFYDD E[1Nal]RP C (SEQ ID NO: 192); C[CF3Nva]YR AC[4MePhe]Y DDE[1Nal] RPC (SEQ ID NO: 193); CLYR ACFYDDE WRPC (SEQ ID NO: 194); CLYR AC[4MePhe]YD DE[1Nal]R PC (SEQ ID NO: 195); and CHY RACFYDD EWRP C (SEQ ID NO: 196), such as: wherein the molecular scaffold is a derivative of TATA which has the following structure:wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of X15-X16-X17-X18-X19-X20-X21-X22-X23-X24-X25-X26-X27-X28-X29(SEQ ID NO: 3) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 65)-A (herein referred to as BCY15206); A-(SEQ ID NO: 65)-A-[Sar6] [KFl] (herein referred to as BCY15194); Ac-(SEQ ID NO: 66)-A-[K(PYA)] (herein referred to as BCY23135); Ac-(SEQ ID NO: 66)-[K(PYA)] (herein referred to as BCY23136); A-(SEQ ID NO: 66)-A-[K(PYA)] (herein referred to as BCY20791); A-(SEQ ID NO: 67)-A (herein referred to as BCY15808);A-(SEQ ID NO: 68)-A (herein referred to as BCY15810); A-(SEQ ID NO: 69)-A (herein referred to as BCY16655); A-(SEQ ID NO: 70)-A (herein referred to as BCY16656); A-(SEQ ID NO: 71)-A (herein referred to as BCY16657); A-(SEQ ID NO: 72)-A (herein referred to as BCY16658); A-(SEQ ID NO: 73)-A (herein referred to as BCY16659); A-(SEQ ID NO: 74)-A (herein referred to as BCY16660); A-(SEQ ID NO: 75)-A (herein referred to as BCY16661); A-(SEQ ID NO: 76)-A (herein referred to as BCY15207); A-(SEQ ID NO: 76)-A-[Sar6]-[KFl] (herein referred to as BCY15195); A-(SEQ ID NO: 76)-A-[K(PYA)] (herein referred to as BCY15750); A-(SEQ ID NO: 77)-A (herein referred to as BCY15811); A-(SEQ ID NO: 78)-A (herein referred to as BCY15812); A-(SEQ ID NO: 79)-A (herein referred to as BCY15813); A-(SEQ ID NO: 80)-A (herein referred to as BCY15814); A-(SEQ ID NO: 80)-A-[Sar6]-[KFl] (herein referred to as BCY15801); Ac-(SEQ ID NO: 80) (herein referred to as BCY17031); A-(SEQ ID NO: 80)-A-[Sar6]-[K(Ac)] (herein referred to as BCY19384); A-(SEQ ID NO: 80)-AGAA AE (herein referred to as BCY19582); A-(SEQ ID NO: 81)-A (herein referred to as BCY17032); A-(SEQ ID NO: 82)-A (herein referred to as BCY17033); A-(SEQ ID NO: 83)-A (herein referred to as BCY17035); A-(SEQ ID NO: 84)-A (herein referred to as BCY17038); A-(SEQ ID NO: 85)-A (herein referred to as BCY17040); A-(SEQ ID NO: 86)-A (herein referred to as BCY17041); A-(SEQ ID NO: 87)-A (herein referred to as BCY17042); A-(SEQ ID NO: 88)-A (herein referred to as BCY17043); Ac-(SEQ ID NO: 89) (herein referred to as BCY19197); A-(SEQ ID NO: 90)-A (herein referred to as BCY16662); A-(SEQ ID NO: 91)-A (herein referred to as BCY16663); A-(SEQ ID NO: 91)-A-[Sar6]-[KFl] (herein referred to as BCY16639); A-(SEQ ID NO: 92)-A (herein referred to as BCY16664); A-(SEQ ID NO: 93)-A (herein referred to as BCY16665); A-(SEQ ID NO: 94)-A (herein referred to as BCY16666); A-(SEQ ID NO: 95)-A (herein referred to as BCY16667); A-(SEQ ID NO: 95)-A-[Sar6]-[KFl] (herein referred to as BCY16643);A-(SEQ ID NO: 95)-A-[K(PYA)] (herein referred to as BCY17238); Ac-(SEQ ID NO: 95) (herein referred to as BCY19193); A-(SEQ ID NO: 96)-A (herein referred to as BCY19192); Ac-(SEQ ID NO: 96) (herein referred to as BCY19196); Ac-(SEQ ID NO: 97) (herein referred to as BCY19194); Ac-(SEQ ID NO: 98) (herein referred to as BCY19195); Ac-(SEQ ID NO: 99) (herein referred to as BCY19198); Ac-(SEQ ID NO: 100) (herein referred to as BCY19199); Ac-(SEQ ID NO: 101) (herein referred to as BCY19200); Ac-(SEQ ID NO: 102) (herein referred to as BCY19203); Ac-(SEQ ID NO: 103) (herein referred to as BCY19205); Ac-(SEQ ID NO: 104) (herein referred to as BCY19206); A-(SEQ ID NO: 105)-A (herein referred to as BCY15208); A-(SEQ ID NO: 105)-A-[K(PYA)] (herein referred to as BCY15751); A-(SEQ ID NO: 106)-A-[K(PYA)] (herein referred to as BCY21608); A-(SEQ ID NO: 107)-A (herein referred to as BCY15209); A-(SEQ ID NO: 107)-A-[Sar6]-[KFl] (herein referred to as BCY15197); A-(SEQ ID NO: 108)-A (herein referred to as BCY15727); A-(SEQ ID NO: 108)-A-[K(PYA)] (herein referred to as BCY17452); Ac-(SEQ ID NO: 108)-[K(PYA)] (herein referred to as BCY19157); Ac-A-(SEQ ID NO: 108)-A-[K(PYA)] (herein referred to as BCY19158); A-(SEQ ID NO: 108)-A-[Sar6]-[(K(Ac)] (herein referred to as BCY19385); A-(SEQ ID NO: 108)-AGAA AE (herein referred to as BCY19580); A-(SEQ ID NO: 108)-KMTH E (herein referred to as BCY21192); A-(SEQ ID NO: 108)-NDSLN (herein referred to as BCY21193 ); A-(SEQ ID NO: 108)-SVNAN (herein referred to as BCY21194); A-(SEQ ID NO: 108)-QGH TPL (herein referred to as BCY21195); A-(SEQ ID NO: 108)-EMEH SN (herein referred to as BCY21196); MR Q-(SEQ ID NO: 108)-ETP (herein referred to as BCY21197); EHM-(SEQ ID NO: 108)-TQ S (herein referred to as BCY21198); EPKR Q-(SEQ ID NO: 108)-A (herein referred to as BCY21199); ANYA N-(SEQ ID NO: 108)-A (herein referred to as BCY21200); DSFH Q-(SEQ ID NO: 108)-A (herein referred to as BCY21201); MRQ-(SEQ ID NO: 108)-ETP-[K(PYA)] (herein referred to as BCY21993); EPKR Q-(SEQ ID NO: 108)-A-[K(PYA)] (herein referred to as BCY21994); Ac-(SEQ ID NO: 108)-A-[K(PYA)] (herein referred to as BCY23137);Ac-(SEQ ID NO: 108)-E-[K(PYA)] (herein referred to as BCY23174); A-(SEQ ID NO: 108)-E-[K(PYA)] (herein referred to as BCY23179); A-(SEQ ID NO: 109)-A-[K(PYA)] (herein referred to as BCY19159); A-(SEQ ID NO: 110)-A-[K(PYA)] (herein referred to as BCY19161); A-(SEQ ID NO: 111)-A-[K(PYA)] (herein referred to as BCY19162); A-(SEQ ID NO: 112)-A-[K(PYA)] (herein referred to as BCY19163); A-(SEQ ID NO: 113)-A-[K(PYA)] (herein referred to as BCY19164); A-(SEQ ID NO: 114)-A-[K(PYA)] (herein referred to as BCY19165); A-(SEQ ID NO: 115)-A-[K(PYA)] (herein referred to as BCY19166); A-(SEQ ID NO: 116)-A-[K(PYA)] (herein referred to as BCY19167); A-(SEQ ID NO: 117)-A (herein referred to as BCY19170); A-(SEQ ID NO: 117)-A-[K(PYA)] (herein referred to as BCY19284); Ac-(SEQ ID NO: 117)-[K(PYA)] (herein referred to as BCY19995); A-(SEQ ID NO: 118)-A-[K(PYA)] (herein referred to as BCY19171); A-(SEQ ID NO: 119)-A-[K(PYA)] (herein referred to as BCY19177); MRQ-(SEQ ID NO: 119)-ETP-[K(PYA)] (herein referred to as BCY21995); EPKR Q-(SEQ ID NO: 119)-A-[K(PYA)] (herein referred to as BCY21996); MRQ-(SEQ ID NO: 119)-ETP (herein referred to as BCY21997); EPKR Q-(SEQ ID NO: 119)-A (herein referred to as BCY21998); Ac-(SEQ ID NO: 119)-[K(PYA)] (herein referred to as BCY22499); A-(SEQ ID NO: 120)-A-[K(PYA)] (herein referred to as BCY19179); A-(SEQ ID NO: 121)-A-[K(PYA)] (herein referred to as BCY19181); A-(SEQ ID NO: 122)-A-[K(PYA)] (herein referred to as BCY19184); A-(SEQ ID NO: 123)-A-[K(PYA)] (herein referred to as BCY19185); A-(SEQ ID NO: 124)-A-[K(PYA)] (herein referred to as BCY19187); A-(SEQ ID NO: 125)-A-[K(PYA)] (herein referred to as BCY19188); A-(SEQ ID NO: 126)-A-[K(PYA)] (herein referred to as BCY19189); [dA]-(SEQ ID NO: 127)-[dA]-[K(PYA)] (herein referred to as BCY20840); A-(SEQ ID NO: 128)-A-[K(PYA)] (herein referred to as BCY21040); A-(SEQ ID NO: 129)-A (herein referred to as BCY21631); A-(SEQ ID NO: 129) (herein referred to as BCY21633); Ac-(SEQ ID NO: 129) (herein referred to as BCY21634); A-(SEQ ID NO: 130) (herein referred to as BCY21635); Ac-(SEQ ID NO: 130) (herein referred to as BCY21636); Ac-(SEQ ID NO: 131)-[K(PYA)] (herein referred to as BCY23702); Ac-(SEQ ID NO: 132)-[K(PYA)] (herein referred to as BCY23703);Ac-(SEQ ID NO: 132)-[K(PYA)-(Triazolyl)-(PEG)2-methyl] (herein referred to as BCY25601); Ac-(SEQ ID NO: 133)-[K(PYA)] (herein referred to as BCY23704); Ac-(SEQ ID NO: 134)-[K(PYA)] (herein referred to as BCY23705); Ac-(SEQ ID NO: 135)-[K(PYA)] (herein referred to as BCY23706); Ac-(SEQ ID NO: 136)-[K(PYA)] (herein referred to as BCY23707); Ac-(SEQ ID NO: 136)-[K(PYA)-(Triazolyl)-(PEG)2-methyl] (herein referred to as BCY25602); A-(SEQ ID NO: 137)-A (herein referred to as BCY15729); A-(SEQ ID NO: 138)-A (herein referred to as BCY15210); A-(SEQ ID NO: 138)-A-[Sar6] -[KFl] (herein referred to as BCY15198); A-(SEQ ID NO: 138)-A-[K(PYA)] (herein referred to as BCY15752); A-(SEQ ID NO: 139)-A (herein referred to as BCY15731); A-(SEQ ID NO: 139)-A-[Sar6] -[KFl] (herein referred to as BCY15730); A-(SEQ ID NO: 140)-A (herein referred to as BCY15733); A-(SEQ ID NO: 141)-A (herein referred to as BCY15735); and A-(SEQ ID NO: 141)-A-[Sar6] -[KFl] (herein referred to as BCY15734); or a modified derivative and / or pharmaceutically acceptable salt thereof, or wherein the molecular scaffold is a derivative of TATB which has the following structure:wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of X15-X16-X17-X18-X19-X20-X21-X22-X23-X24-X25-X26-X27-X28-X29(SEQ ID NO: 3) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 142)-A (herein referred to as BCY17001); A-(SEQ ID NO: 143)-A (herein referred to as BCY18128); A-(SEQ ID NO: 143)-A-[K(PYA)] (herein referred to as BCY19743); A-(SEQ ID NO: 144)-A (herein referred to as BCY18129); A-(SEQ ID NO: 144)-A-[K(PYA)] (herein referred to as BCY19744); Ac-A-(SEQ ID NO: 144)-A (herein referred to as BCY24131 ); Ac-(SEQ ID NO: 144) (herein referred to as BCY24135);A-(SEQ ID NO: 144) (herein referred to as BCY24450); Ac-A-(SEQ ID NO: 144) (herein referred to as BCY24451); (SEQ ID NO: 144)-A (herein referred to as BCY24452); Ac-(SEQ ID NO: 144)-A (herein referred to as BCY24453); AHG G-(SEQ ID NO: 144)-EVHA (herein referred to as BCY25863 ); AI KP-(SEQ ID NO: 144)-QHEA (herein referred to as BCY25864); ADST-(SEQ ID NO: 144)-QH PA (herein referred to as BCY25865); ALNG-(SEQ ID NO: 144)-PLS A (herein referred to as BCY25866); ALNG-(SEQ ID NO: 144)-PLS A-[K(PYA)] (herein referred to as BCY28840); A-(SEQ ID NO: 145)-A (herein referred to as BCY24442); A-(SEQ ID NO: 146)-A (herein referred to as BCY24443); A-(SEQ ID NO: 147)-A (herein referred to as BCY24444); A-(SEQ ID NO: 148)-A (herein referred to as BCY24445); A-(SEQ ID NO: 149)-A (herein referred to as BCY24456); A-(SEQ ID NO: 150)-A (herein referred to as BCY24457); A-(SEQ ID NO: 151)-A (herein referred to as BCY24458); A-(SEQ ID NO: 152)-A (herein referred to as BCY24459); A-(SEQ ID NO: 153)-A (herein referred to as BCY24462); A-(SEQ ID NO: 154)-A (herein referred to as BCY24466); A-(SEQ ID NO: 155)-A (herein referred to as BCY24467); A-(SEQ ID NO: 156)-A (herein referred to as BCY24468); A-(SEQ ID NO: 157)-A (herein referred to as BCY24469); A-(SEQ ID NO: 158)-A (herein referred to as BCY24471); A-(SEQ ID NO: 159)-A (herein referred to as BCY24472); A-(SEQ ID NO: 160)-A (herein referred to as BCY24473); A-(SEQ ID NO: 161)-A (herein referred to as BCY24474); A-(SEQ ID NO: 162)-A (herein referred to as BCY24475); A-(SEQ ID NO: 163)-A (herein referred to as BCY24477); A-(SEQ ID NO: 164)-A (herein referred to as BCY24478); A-(SEQ ID NO: 165)-A (herein referred to as BCY24479); A-(SEQ ID NO: 166)-A (herein referred to as BCY24480); A-(SEQ ID NO: 167)-A (herein referred to as BCY24481); A-(SEQ ID NO: 168)-A (herein referred to as BCY24482); A-(SEQ ID NO: 169)-A (herein referred to as BCY24483); A-(SEQ ID NO: 170)-A (herein referred to as BCY24484); A-(SEQ ID NO: 171)-A (herein referred to as BCY24485);A-(SEQ ID NO: 172)-A (herein referred to as BCY24486); A-(SEQ ID NO: 173)-A (herein referred to as BCY24487); A-(SEQ ID NO: 174)-A (herein referred to as BCY24488); A-(SEQ ID NO: 175)-A (herein referred to as BCY24489); A-(SEQ ID NO: 176)-A (herein referred to as BCY24490); A-(SEQ ID NO: 177)-A (herein referred to as BCY24491); A-(SEQ ID NO: 178)-A (herein referred to as BCY24492); A-(SEQ ID NO: 179)-A (herein referred to as BCY24493); A-(SEQ ID NO: 180)-A (herein referred to as BCY24495); A-(SEQ ID NO: 181)-A (herein referred to as BCY24496); A-(SEQ ID NO: 182)-A (herein referred to as BCY24497); A-(SEQ ID NO: 183)-A (herein referred to as BCY24498); A-(SEQ ID NO: 184)-A (herein referred to as BCY24499); A-(SEQ ID NO: 185)-A (herein referred to as BCY24500); A-(SEQ ID NO: 186)-A (herein referred to as BCY24501); A-(SEQ ID NO: 187)-A (herein referred to as BCY24503); A-(SEQ ID NO: 188)-A (herein referred to as BCY24504); A-(SEQ ID NO: 189)-A (herein referred to as BCY24505); A-(SEQ ID NO: 190)-A (herein referred to as BCY24506); A-(SEQ ID NO: 191)-A (herein referred to as BCY24509); ALNG-(SEQ ID NO: 192)-PLS A (herein referred to as BCY28838); ALNG-(SEQ ID NO: 192)-PLS A-[K(PYA)] (herein referred to as BCY28841); ALNG-(SEQ ID NO: 193)-PLS A (herein referred to as BCY28839); ALNG-(SEQ ID NO: 193)-PLS A-[K(PYA)] (herein referred to as BCY28842); ALEQ N-(SEQ ID NO: 194)-A (herein referred to as BCY25861); ALEQ N-(SEQ ID NO: 194)-A-[K(PYA)] (herein referred to as BCY28843); ALEQ N-(SEQ ID NO: 195)-A (herein referred to as BCY28844 ); ALEQ N-(SEQ ID NO: 195)-A-[K(PYA)] (herein referred to as BCY28845); and AHAG T-(SEQ ID NO: 196)-A (herein referred to as BCY25859 ); or a modified derivative and / or pharmaceutically acceptable salt thereof.

7. The bicyclic peptide ligand according to claim 3, wherein the peptide ligand of C-Q-P-T- X30-X31-C-X32-X33-X34-X35-X36-X37-C (SEQ ID NO: 4) comprises an amino acid sequence selected from: CQ PTPRCPFSTWPC (herein referred to as SEQ ID NO: 197);CQ PTPQCPY STWPC (herein referred to as SEQ ID NO: 198, herein referred to as BCY20723 when complexed with a derivative of TATB which has the following structure:wherein * denotes the point of attachment of the three cysteine residues); CQ PT[HyP]QCPY STWPC (herein referred to as SEQ ID NO: 199); CQ PT[Cis-HyP]QCPYS TWPC (herein referred to as SEQ ID NO: 200); CQ PT[Pip]QC PYSTWPC (herein referred to as SEQ ID NO: 201); CQ PTPECPYS TWPC (herein referred to as SEQ ID NO: 202); CQ PTPQC[HyP]Y STWPC (herein referred to as SEQ ID NO: 203); CQ PTPQC[Cis-HyP]YS TWPC (herein referred to as SEQ ID NO: 204); CQ PTPQC[Aze]YSTWPC (herein referred to as SEQ ID NO: 205); CQ PTPQCP[2Nal] STWPC (herein referred to as SEQ ID NO: 206); CQ PTPQCP[4tBuPhe]STWPC (herein referred to as SEQ ID NO: 207); CQ PTPQCP[4FPhe]S TWPC (herein referred to as SEQ ID NO: 208); CQ PTPQCP[3FTyr] STWP C (herein referred to as SEQ ID NO: 209); CQ PTPQCP[2FTyr] STWP C (herein referred to as SEQ ID NO: 210); CQ PTPQCPY [Dap]TWPC (herein referred to as SEQ ID NO: 211); CQ PTPQCPY S[Dap]WPC (herein referred to as SEQ ID NO: 212); CQ PTPQCPY ST[2Nal]PC (herein referred to as SEQ ID NO: 213); CQ PTPQCPY ST[1Nal]PC (herein referred to as SEQ ID NO: 214); CQ PTPQCPY ST[6FTrp]PC (herein referred to as SEQ ID NO: 215); CQ PTPQCPY ST[5FTrp]PC (herein referred to as SEQ ID NO: 216); CQ PTPQCPY ST[6ClTrp]PC (herein referred to as SEQ ID NO: 217); CQ PTPQCPY ST[4MeoTrp]P C (herein referred to as SEQ ID NO: 218); CQ PTPQCPY ST[5MeoTrp]P C (herein referred to as SEQ ID NO: 219); CQ PTPQCPY ST[Trp(S)]PC (herein referred to as SEQ ID NO: 220); CQ PTPQCPY ST[AzaTrp]PC (herein referred to as SEQ ID NO: 221); CQ PTPQCPY STW[HyP]C (herein referred to as SEQ ID NO: 222); CQ PTPQCPY STW[Cis-HyP]C (herein referred to as SEQ ID NO: 223); CQ PTPQCPY STW[Aze]C (herein referred to as SEQ ID NO: 224);CQ PTPQCPY STW[Pip] C (herein referred to as SEQ ID NO: 225); and CQ PTPECPYN TWPC (herein referred to as SEQ ID NO: 226), such as wherein the molecular scaffold is a derivative of TATB which has the following structure:wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of C-Q-P-T-X30-X31-C-X32-X33-X34-X35-X36-X37-C (SEQ ID NO: 4) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 197)-A (herein referred to as BCY16999); A-(SEQ ID NO: 197)-A-[K(PYA)] (herein referred to as BCY17693); A-(SEQ ID NO: 197)-A-[Sar6]-[K(Ac)] (herein referred to as BCY19387); A-(SEQ ID NO: 198)-A (herein referred to as BCY18126); Ac-A-(SEQ ID NO: 198)-A (herein referred to as BCY20725); A-(SEQ ID NO: 198)-NLNLK (herein referred to as BCY21770 ); VNEN I-(SEQ ID NO: 198)-A (herein referred to as BCY21771); A-(SEQ ID NO: 198)-RNPH D (herein referred to as BCY21772); A-(SEQ ID NO: 198)-IHN NG (herein referred to as BCY21774); TNEG I-(SEQ ID NO: 198)-A (herein referred to as BCY21778); VNEN I-(SEQ ID NO: 198)-A-[K(PYA)] (herein referred to as BCY23767); A-(SEQ ID NO: 199)-A (herein referred to as BCY20731); A-(SEQ ID NO: 200)-A (herein referred to as BCY20732); A-(SEQ ID NO: 201)-A (herein referred to as BCY20734); A-(SEQ ID NO: 202)-A (herein referred to as BCY20735); A-(SEQ ID NO: 203)-A (herein referred to as BCY20736); A-(SEQ ID NO: 204)-A (herein referred to as BCY20737); A-(SEQ ID NO: 205)-A (herein referred to as BCY20738); A-(SEQ ID NO: 206)-A (herein referred to as BCY20741); A-(SEQ ID NO: 207)-A (herein referred to as BCY20742); A-(SEQ ID NO: 208)-A (herein referred to as BCY20743); A-(SEQ ID NO: 209)-A (herein referred to as BCY20746);A-(SEQ ID NO: 210)-A (herein referred to as BCY20747); A-(SEQ ID NO: 211)-A (herein referred to as BCY20748); A-(SEQ ID NO: 212)-A (herein referred to as BCY20749); A-(SEQ ID NO: 213)-A (herein referred to as BCY20751); A-(SEQ ID NO: 214)-A (herein referred to as BCY20752); A-(SEQ ID NO: 215)-A (herein referred to as BCY20756); A-(SEQ ID NO: 216)-A (herein referred to as BCY20757); A-(SEQ ID NO: 217)-A (herein referred to as BCY20758); A-(SEQ ID NO: 218)-A (herein referred to as BCY20759); A-(SEQ ID NO: 219)-A (herein referred to as BCY20760); A-(SEQ ID NO: 220)-A (herein referred to as BCY20761); A-(SEQ ID NO: 221)-A (herein referred to as BCY20762); A-(SEQ ID NO: 222)-A (herein referred to as BCY20763); A-(SEQ ID NO: 223)-A (herein referred to as BCY20764); A-(SEQ ID NO: 224)-A (herein referred to as BCY20765); A-(SEQ ID NO: 225)-A (herein referred to as BCY20766); A-(SEQ ID NO: 226)-A (herein referred to as BCY18127); and A-(SEQ ID NO: 226)-A-[K(PYA)] (herein referred to as BCY19742); or a modified derivative and / or pharmaceutically acceptable salt thereof.

8. The bicyclic peptide ligand according to claim 3, wherein the peptide ligand of C-Y-Y-X38- X39-X40-Y-A-C-L-D-C (SEQ ID NO: 5) comprises an amino acid sequence selected from: CYYP DYYACLD C (herein referred to as SEQ ID NO: 227); CYYE NYYACLD C (herein referred to as SEQ ID NO: 228); and CYYP DWYA CLDC (herein referred to as SEQ ID NO: 229), such as wherein the molecular scaffold is a tri-substituted 2,4,6-tris(bromomethyl)-s-triazine derivative of TBMT, or TCTZ, having the following structure:wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of C-Y-Y-X38-X39-X40-Y-A-C-L-D-C (SEQ ID NO: 5) additionally comprises N- and / or C- terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 227)-A (herein referred to as BCY17007); A-(SEQ ID NO: 228)-A (herein referred to as BCY18135); A-(SEQ ID NO: 229)-A (herein referred to as BCY18136); and A-(SEQ ID NO: 229)-A-[K(PYA)] (herein referred to as BCY19747); or a modified derivative and / or pharmaceutically acceptable salt thereof.

9. The bicyclic peptide ligand according to claim 3, wherein the peptide ligand of X41-X42-X43- X44-X45-X46-X47-X48-X49-C-X50-X51-X52-X53-X54(SEQ ID NO: 6) comprises an amino acid sequence selected from: CNN PVMTYWCTKG IC (herein referred to as SEQ ID NO: 230); CNN PVMTYWCEKG IC (herein referred to as SEQ ID NO: 231); CDN EVITYWCTKG IC (herein referred to as SEQ ID NO: 232); CDN EV[tBuAla]TYWCTKGI C (herein referred to as SEQ ID NO: 233); CDN EVFTYWCTKGI C (herein referred to as SEQ ID NO: 234); CDN EV[Cba]TYWCTKGI C (herein referred to as SEQ ID NO: 235); CDN EVITY[2Nal] CTKG IC (herein referred to as SEQ ID NO: 236); CDN EVITY[1Nal] CTKG IC (herein referred to as SEQ ID NO: 237); CDN EVITYWCT[Orn]GI C (herein referred to as SEQ ID NO: 238); CDN EVITYWCT[HArg]GI C (herein referred to as SEQ ID NO: 239); CDN EVITYWCTK[dA]I C (herein referred to as SEQ ID NO: 240); CDN EVITYWCTKG [tBuGly]C (herein referred to as SEQ ID NO: 241); CDN EVIT[DOPA]WCTKGI C (herein referred to as SEQ ID NO: 242); CDN PVFTYWCTKGI C (herein referred to as SEQ ID NO: 243); CNN PVMAY WCTKG IC (herein referred to as SEQ ID NO: 244); CPN PVITYWCTKG IC (herein referred to as SEQ ID NO: 245); CDN EVITYWCQ MGVC (herein referred to as SEQ ID NO: 246); CDN EVITYWCQ RGVC (herein referred to as SEQ ID NO: 247); CDN EVITYWCM RGI C (herein referred to as SEQ ID NO: 248); CDN EVITYWCQ RGIC (herein referred to as SEQ ID NO: 249); CDN EVITY[6FTrp] CQR GIC (herein referred to as SEQ ID NO: 250); CDN EVITY[5FTrp] CQR GIC (herein referred to as SEQ ID NO: 251); CDN EVITY[5MeoTrp]CQ RGI C (herein referred to as SEQ ID NO: 252); CDN EVITY[Trp(S)]CQ RGI C (herein referred to as SEQ ID NO: 253);CDN EVITY[AzaTrp] CQR GIC (herein referred to as SEQ ID NO: 254); CDN EVITYWCQ [HArg]G IC (herein referred to as SEQ ID NO: 255); CDN EVITYWCQ [Cit]G IC (herein referred to as SEQ ID NO: 256); CDN EVFEYWCTKGI C (herein referred to as SEQ ID NO: 257); CDN EVITYWCER GIC (herein referred to as SEQ ID NO: 258); CDN EVITYWCEM GIC (herein referred to as SEQ ID NO: 259); CSN PVFAYWCSRQM C (herein referred to as SEQ ID NO: 260); CSN PVFAYWCERGI C (herein referred to as SEQ ID NO: 261, herein referred to as BCY21615 when complexed with a tri-substituted 2,4,6-tris(bromomethyl)-s-triazine derivative of TBMT having the following structure:wherein * denotes the point of attachment of the three cysteine residues); CSN PVFAYWCER[K(PYA)]IC (herein referred to as SEQ ID NO: 262); CSN PVFAYWCER[dK(PYA)]IC (herein referred to as SEQ ID NO: 263); CSN PVFAYWCER[S-aMeLys(PYA)]I C (herein referred to as SEQ ID NO: 264); CSN PVFAYWCER[R-aMeLys(PYA)]I C (herein referred to as SEQ ID NO: 265); C[K(PYA)]NPVFAY WCER GIC (herein referred to as SEQ ID NO: 266); CSN PVFAY[5FTrp] CERGI C (herein referred to as SEQ ID NO: 267); CSN PVFAYWCERGI [Cysam] (herein referred to as SEQ ID NO: 268, herein referred to as BCY21623 when complexed with a tri-substituted 2,4,6-tris(bromomethyl)-s-triazine derivative of TBMT having the following structure:wherein * denotes the point of attachment of the three cysteine residues); C[K(PYA)]NPVFAY WCER GI[Cysam] (herein referred to as SEQ ID NO: 269); CSN PVFAYWC[Dap]RGI C (herein referred to as SEQ ID NO: 270); CKN PVFAYWC[PG]RG IC (herein referred to as SEQ ID NO: 271);CEN PVFAYWCERGI C (herein referred to as SEQ ID NO: 272); C[dA]NP VFAYWCERGI C (herein referred to as SEQ ID NO: 273); CG NPVFAYWCERG IC (herein referred to as SEQ ID NO: 274); C[Aib] NPVFAYWCERG IC (herein referred to as SEQ ID NO: 275); CSN [trans-4FlPro]VFAYWCERG IC (herein referred to as SEQ ID NO: 276); CSN [4FlPro]V FAYWC ERGI C (herein referred to as SEQ ID NO: 277); CSN [HyP]VFAYWCERGI C (herein referred to as SEQ ID NO: 278); CSN [Cis-HyP]VFAYWCERGI C (herein referred to as SEQ ID NO: 279); CSN P[HSer]FA YWCE RGI C (herein referred to as SEQ ID NO: 280); CSN PV[2FPhe]AYWCERG IC (herein referred to as SEQ ID NO: 281); CSN PV[4CF3Phe]AYWCERG IC (herein referred to as SEQ ID NO: 282); CSN PVFSYWCERGI C (herein referred to as SEQ ID NO: 283); CSN PVF[Dap]YWCERGI C (herein referred to as SEQ ID NO: 284); CSN PVF[CF3Ala]Y WCER GIC (herein referred to as SEQ ID NO: 285); CSN PVFA[2FTyr]WCERG IC (herein referred to as SEQ ID NO: 286); CSN PVFA[3FTyr]WCERG IC (herein referred to as SEQ ID NO: 287); CSN PVFAY[4FTrp] CERGI C (herein referred to as SEQ ID NO: 288); CSN PVFAYWCE[Cit]GI C (herein referred to as SEQ ID NO: 289); CSN PVFAYWCER[dA]I C (herein referred to as SEQ ID NO: 290); CSN PVFAYWCERG[Nva]C (herein referred to as SEQ ID NO: 291); CSN PVFAYWCERG[Nle] C (herein referred to as SEQ ID NO: 292); CSN PVFAYWCERG[EPA] C (herein referred to as SEQ ID NO: 293); CSN PVFAYWCERG[tBuGly] C (herein referred to as SEQ ID NO: 294); CSN [4FlPro]V FAY[5FTrp]C ERG[EPA] C (herein referred to as SEQ ID NO: 295); C[Aib] N[4FlPro]VFAY[5FTrp] CERG[EPA] C (herein referred to as SEQ ID NO: 296); C[dS]N[4FlPro]V FAY[5FTrp]CE RG[EPA]C (herein referred to as SEQ ID NO: 297); C[K(PYA)]N[4FlPro]VFAY[5FTrp] CERG [EPA]C (herein referred to as SEQ ID NO: 298); C[dK(PYA)]N[4FlPro]VFAY[5FTrp] CERG [EPA]C (herein referred to as SEQ ID NO: 299); [dC]SN[4FlPro]V FAY[5FTrp]CE RG[EPA]C (herein referred to as SEQ ID NO: 300); CSN [4FlPro]V FAY[5FTrp]C ERG[EPA] [dC] (herein referred to as SEQ ID NO: 301); [dC]SN[4FlPro]V FAY[5FTrp]CE RG[EPA][dC] (herein referred to as SEQ ID NO: 302); CSN PVFAYWCSRNLC (herein referred to as SEQ ID NO: 303); CSN PVFAYWCSRGLC (herein referred to as SEQ ID NO: 304); CTTDM MWKVCRTLD C (herein referred to as SEQ ID NO: 305); CATD HMWKVCRTLDC (herein referred to as SEQ ID NO: 306); CKTD AMWKVCRTLDC (herein referred to as SEQ ID NO: 307);CSTD QMWKVCRTLD C (herein referred to as SEQ ID NO: 308); CSTD YMWKVCRTLDC (herein referred to as SEQ ID NO: 309, herein referred to as BCY23141 when complexed with a tri-substituted 2,4,6-tris(bromomethyl)-s-triazine derivative of TBMT having the following structure:wherein * denotes the point of attachment of the three cysteine residues); CSTD Y[Nle]WKVCRTLD C (herein referred to as SEQ ID NO: 310); CATD YMWKVCRTLDC (herein referred to as SEQ ID NO: 311); CSTD AMWKVCRTLDC (herein referred to as SEQ ID NO: 312); CSTD YAWKV CRTLDC (herein referred to as SEQ ID NO: 313); CSTD YMWKACRTLDC (herein referred to as SEQ ID NO: 314); CSTD YMWKVCRALD C (herein referred to as SEQ ID NO: 315); CSTD YMWKVCRTAD C (herein referred to as SEQ ID NO: 316); C[CF3Ala]TDYMWKVC RTLDC (herein referred to as SEQ ID NO: 317); C[HSer]TDYM WKVC RTLDC (herein referred to as SEQ ID NO: 318); CTTDY MWK VCRTLDC (herein referred to as SEQ ID NO: 319); C[3HyV]TDY MWKVCRTLDC (herein referred to as SEQ ID NO: 320); CS[3HyV]D YMWKVCRTLD C (herein referred to as SEQ ID NO: 321); C[Dap]TDY MWKVCRTLDC (herein referred to as SEQ ID NO: 322); CSTD [4FPhe]MWK VCRTLDC (herein referred to as SEQ ID NO: 323); CSTD [1Nal]MWKVCR TLDC (herein referred to as SEQ ID NO: 324); CSTD [2Nal]MWKVCR TLDC (herein referred to as SEQ ID NO: 325); CSTD [26DiMeTyr]MWKVCRTLDC (herein referred to as SEQ ID NO: 326); CSTD [3FTyr]MWKVCRTLD C (herein referred to as SEQ ID NO: 327); CSTD [2FTyr]MWKVCRTLD C (herein referred to as SEQ ID NO: 328); CSTD [DOPA]M WKVC RTLDC (herein referred to as SEQ ID NO: 329); CSTD Y[Nva]WKVC RTLDC (herein referred to as SEQ ID NO: 330); CSTD Y[TfNle]WKVC RTLDC (herein referred to as SEQ ID NO: 331); CSTD YEWKV CRTLDC (herein referred to as SEQ ID NO: 332); CSTD Y[CF3Nva]WKV CRTLDC (herein referred to as SEQ ID NO: 333); CSTD YM[1Nal] KVCRTLDC (herein referred to as SEQ ID NO: 334);CSTD YM[4FTrp]K VCRTLDC (herein referred to as SEQ ID NO: 335); CSTD YM[5FTrp]K VCRTLDC (herein referred to as SEQ ID NO: 336); CSTD YM[6FTrp]K VCRTLDC (herein referred to as SEQ ID NO: 337); CSTD YM[7FTrp]K VCRTLDC (herein referred to as SEQ ID NO: 338); CSTD YM[2MeTrp]KVCRTLD C (herein referred to as SEQ ID NO: 339); CSTD YM[4MeTrp]KVCRTLD C (herein referred to as SEQ ID NO: 340); CSTD YM[5MeTrp]KVCRTLD C (herein referred to as SEQ ID NO: 341); CSTD YM[6MeTrp]KVCRTLD C (herein referred to as SEQ ID NO: 342); CSTD YM[7MeTrp]KVCRTLD C (herein referred to as SEQ ID NO: 343); CSTD YM[AzaTrp]K VCRTLDC (herein referred to as SEQ ID NO: 344); CSTD YMW[HArg]VC RTLDC (herein referred to as SEQ ID NO: 345); CSTD YMW[Orn]VC RTLDC (herein referred to as SEQ ID NO: 346); CSTD YMW[Agb]VCRTLDC (herein referred to as SEQ ID NO: 347); CSTD YMWK[tBuGly]CRTLDC (herein referred to as SEQ ID NO: 348); CSTD YMWK[Cbg]CRTLDC (herein referred to as SEQ ID NO: 349); CSTD YMWK[C5g]CRTLDC (herein referred to as SEQ ID NO: 350); CSTD YMWK[3HyV]CRTLDC (herein referred to as SEQ ID NO: 351); CSTD YMWKVC[HArg]TLDC (herein referred to as SEQ ID NO: 352); CSTD YMWKVC[Arg(Me)]TLDC (herein referred to as SEQ ID NO: 353); CSTD YMWKVCR[3HyV]LD C (herein referred to as SEQ ID NO: 354); CSTD YMWKVCRT[tBuAla]DC (herein referred to as SEQ ID NO: 355); CSTD YMWKVCRT[Cba]D C (herein referred to as SEQ ID NO: 356); CSTD YMWKVCRT[Nva]DC (herein referred to as SEQ ID NO: 357); CSTD YMWKVCRT[Nle] DC (herein referred to as SEQ ID NO: 358); CTTDM AWR DCRTLDC (herein referred to as SEQ ID NO: 359); CTTDM AWR LCRTLDC (herein referred to as SEQ ID NO: 360); CTTDM VWK VCRTLDC (herein referred to as SEQ ID NO: 361); CVTD YMWKVCRTLDC (herein referred to as SEQ ID NO: 362); CYTD SMWKVCRTLDC (herein referred to as SEQ ID NO: 363); CTTDM MWKVCREP DC (herein referred to as SEQ ID NO: 364); CTTDM MWKVCRSM DC (herein referred to as SEQ ID NO: 365); and CTTDMMWKVCRTLDC (herein referred to as SEQ ID NO: 366), such as wherein the molecular scaffold is a derivative of TATA which has the following structure:wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of X41-X42-X43-X44-X45-X46-X47-X48-X49-C-X50-X51-X52-X53-X54(SEQ ID NO: 6) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 230)-A (herein referred to as BCY15211); A-(SEQ ID NO: 230)-A-[Sar6]-[KFl] (herein referred to as BCY15199); A-(SEQ ID NO: 231)-A (herein referred to as BCY15737); A-(SEQ ID NO: 232)-A (herein referred to as BCY15739); A-(SEQ ID NO: 232)-A-[Sar6]-[KFl] (herein referred to as BCY15738); A-(SEQ ID NO: 232)-A-[Sar6]-[K(Ac)] (herein referred to as BCY19386); A-(SEQ ID NO: 232)-AGAA AE (herein referred to as BCY19581); A-(SEQ ID NO: 233)-A (herein referred to as BCY17047); A-(SEQ ID NO: 234)-A (herein referred to as BCY17049); A-(SEQ ID NO: 235)-A (herein referred to as BCY17051); A-(SEQ ID NO: 236)-A (herein referred to as BCY17055); A-(SEQ ID NO: 237)-A (herein referred to as BCY17056); A-(SEQ ID NO: 238)-A (herein referred to as BCY17057); A-(SEQ ID NO: 239)-A (herein referred to as BCY17058); A-(SEQ ID NO: 240)-A (herein referred to as BCY17059); A-(SEQ ID NO: 241)-A (herein referred to as BCY17061); A-(SEQ ID NO: 242)-A (herein referred to as BCY17656); A-(SEQ ID NO: 243)-A (herein referred to as BCY15741); A-(SEQ ID NO: 244)-A (herein referred to as BCY15743); A-(SEQ ID NO: 245)-A (herein referred to as BCY15745); A-(SEQ ID NO: 246)-A (herein referred to as BCY16668); A-(SEQ ID NO: 247)-A (herein referred to as BCY16669); A-(SEQ ID NO: 248)-A (herein referred to as BCY16670); A-(SEQ ID NO: 249)-A (herein referred to as BCY16671); A-(SEQ ID NO: 249)-A-[Sar6]-[KFl] (herein referred to as BCY16647);Ac-A-(SEQ ID NO: 249)-A (herein referred to as BCY19586 ); A-(SEQ ID NO: 250)-A (herein referred to as BCY18510); A-(SEQ ID NO: 251)-A (herein referred to as BCY18511); A-(SEQ ID NO: 251)-A-[K(PYA)] (herein referred to as BCY25826); A-(SEQ ID NO: 252)-A (herein referred to as BCY18514); A-(SEQ ID NO: 253)-A (herein referred to as BCY18515); A-(SEQ ID NO: 254)-A (herein referred to as BCY18518); A-(SEQ ID NO: 255)-A (herein referred to as BCY18519); A-(SEQ ID NO: 256)-A (herein referred to as BCY18520); A-(SEQ ID NO: 257)-A (herein referred to as BCY16672); A-(SEQ ID NO: 258)-A (herein referred to as BCY16673); A-(SEQ ID NO: 258)-A-[Sar6]-[KFl] (herein referred to as BCY16649); A-(SEQ ID NO: 258)-A-[K(PYA)] (herein referred to as BCY17237); Ac-A-(SEQ ID NO: 258)-A (herein referred to as BCY19585); and A-(SEQ ID NO: 259)-A (herein referred to as BCY16674); or a modified derivative and / or pharmaceutically acceptable salt thereof, or wherein the molecular scaffold is a tri-substituted 2,4,6-tris(bromomethyl)-s-triazine derivative of TBMT, or TCTZ, having the following structure:wherein * denotes the point of attachment of the three cysteine residues, and the peptide ligand of X41-X42-X43-X44-X45-X46-X47-X48-X49-C-X50-X51-X52-X53-X54(SEQ ID NO: 6) additionally comprises N- and / or C-terminal additions and comprises an amino acid sequence which is selected from: A-(SEQ ID NO: 260)-A (herein referred to as BCY17002); A-(SEQ ID NO: 260)-A-[K(PYA)] (herein referred to as BCY19745); A-(SEQ ID NO: 261)-A (herein referred to as BCY18130); A-(SEQ ID NO: 261)-A-[K(PYA)] (herein referred to as BCY20847); [PYA]-A-(SEQ ID NO: 261)-A (herein referred to as BCY20852); Ac-(SEQ ID NO: 261) (herein referred to as BCY21616); A-(SEQ ID NO: 261) (herein referred to as BCY21617);Ac-A-(SEQ ID NO: 261) (herein referred to as BCY21618); [PYA]-(SEQ ID NO: 261) (herein referred to as BCY21619); [GuanAc]-(SEQ ID NO: 261)-A (herein referred to as BCY23043); A-(SEQ ID NO: 261)-[CF3Ala] (herein referred to as BCY23080); A-(SEQ ID NO: 261)-S (herein referred to as BCY23081); A-(SEQ ID NO: 262)-A (herein referred to as BCY20848); A-(SEQ ID NO: 263)-A (herein referred to as BCY20849); A-(SEQ ID NO: 264)-A (herein referred to as BCY20850); A-(SEQ ID NO: 265)-A (herein referred to as BCY20851); A-(SEQ ID NO: 266)-A (herein referred to as BCY20853); A-(SEQ ID NO: 266) (herein referred to as BCY21620); A-(SEQ ID NO: 267)-A (herein referred to as BCY21622); A-(SEQ ID NO: 267)-A-[K(PYA)] (herein referred to as BCY21607); Ac-(SEQ ID NO: 268) (herein referred to as BCY21624); A-(SEQ ID NO: 268) (herein referred to as BCY21625); [PYA]-(SEQ ID NO: 268) (herein referred to as BCY21626); A-(SEQ ID NO: 269) (herein referred to as BCY21627); Ac-(SEQ ID NO: 270) (herein referred to as BCY22879); Ac-(SEQ ID NO: 271) (herein referred to as BCY22880); A-(SEQ ID NO: 272)-A (herein referred to as BCY23044); A-(SEQ ID NO: 273)-A (herein referred to as BCY23045); A-(SEQ ID NO: 274)-A (herein referred to as BCY23046); A-(SEQ ID NO: 275)-A (herein referred to as BCY23047); A-(SEQ ID NO: 276)-A (herein referred to as BCY23050); A-(SEQ ID NO: 277)-A (herein referred to as BCY23051); A-(SEQ ID NO: 278)-A (herein referred to as BCY23052); A-(SEQ ID NO: 279)-A (herein referred to as BCY23053); A-(SEQ ID NO: 280)-A (herein referred to as BCY23054); A-(SEQ ID NO: 281)-A (herein referred to as BCY23058); A-(SEQ ID NO: 282)-A (herein referred to as BCY23059); A-(SEQ ID NO: 283)-A (herein referred to as BCY23062); A-(SEQ ID NO: 284)-A (herein referred to as BCY23063); A-(SEQ ID NO: 285)-A (herein referred to as BCY23064); A-(SEQ ID NO: 286)-A (herein referred to as BCY23066); A-(SEQ ID NO: 287)-A (herein referred to as BCY23067); A-(SEQ ID NO: 288)-A (herein referred to as BCY23068);A-(SEQ ID NO: 289)-A (herein referred to as BCY23071); A-(SEQ ID NO: 290)-A (herein referred to as BCY23072); A-(SEQ ID NO: 291)-A (herein referred to as BCY23073); A-(SEQ ID NO: 292)-A (herein referred to as BCY23074); A-(SEQ ID NO: 293)-A (herein referred to as BCY23075); A-(SEQ ID NO: 294)-A (herein referred to as BCY23079); [GuanAc]-(SEQ ID NO: 295)-COOH (herein referred to as BCY27058); [GuanAc]-(SEQ ID NO: 295) (herein referred to as BCY27059); [CIA]-[K(PYA)]-(SEQ ID NO: 295)-A (herein referred to as BCY27064); [CIA]-[dK(PYA)]-(SEQ ID NO: 295)-A (herein referred to as BCY27065); [GuanAc]-(SEQ ID NO: 296) (herein referred to as BCY27060); [GuanAc]-(SEQ ID NO: 297) (herein referred to as BCY27061); [GuanAc]-(SEQ ID NO: 298) (herein referred to as BCY27062); [GuanAc]-(SEQ ID NO: 299) (herein referred to as BCY27063); [GuanAc]-(SEQ ID NO: 300) (herein referred to as BCY27066); [GuanAc]-(SEQ ID NO: 301) (herein referred to as BCY27067); [GuanAc]-(SEQ ID NO: 302) (herein referred to as BCY27068); A-(SEQ ID NO: 303)-A (herein referred to as BCY18131); A-(SEQ ID NO: 304)-A (herein referred to as BCY18132); A-(SEQ ID NO: 305)-A-[K(PYA)] (herein referred to as BCY19588); A-(SEQ ID NO: 306)-A (herein referred to as BCY19933); A-(SEQ ID NO: 307)-A (herein referred to as BCY19934); A-(SEQ ID NO: 308)-A (herein referred to as BCY19935); A-(SEQ ID NO: 309)-A (herein referred to as BCY19936); A-(SEQ ID NO: 309)-A-[K(PYA)] (herein referred to as BCY21606); Ac-(SEQ ID NO: 309) (herein referred to as BCY23139); Ac-A-(SEQ ID NO: 309)-A (herein referred to as BCY23140); [dA]-(SEQ ID NO: 309)-A (herein referred to as BCY32061); A-(SEQ ID NO: 309) (herein referred to as BCY32074); Ac-A-(SEQ ID NO: 309) (herein referred to as BCY32075); (SEQ ID NO: 309)-A (herein referred to as BCY32076); Ac-(SEQ ID NO: 309)-A (herein referred to as BCY32077); A-(SEQ ID NO: 309)-A-[dK(PYA)] (herein referred to as BCY32126); A-(SEQ ID NO: 309)-[K(PYA)] (herein referred to as BCY32127); A-(SEQ ID NO: 309)-[dK(PYA)] (herein referred to as BCY32128); A-(SEQ ID NO: 310)-A (herein referred to as BCY23138);A-(SEQ ID NO: 310)-A-[K(PYA)] (herein referred to as BCY24613); A-(SEQ ID NO: 311)-A (herein referred to as BCY32062); A-(SEQ ID NO: 312)-A (herein referred to as BCY32065); A-(SEQ ID NO: 313)-A (herein referred to as BCY32066); A-(SEQ ID NO: 314)-A (herein referred to as BCY32069); A-(SEQ ID NO: 315)-A (herein referred to as BCY32071); A-(SEQ ID NO: 316)-A (herein referred to as BCY32072); A-(SEQ ID NO: 317)-A (herein referred to as BCY32078); A-(SEQ ID NO: 318)-A (herein referred to as BCY32079); A-(SEQ ID NO: 319)-A (herein referred to as BCY32080); A-(SEQ ID NO: 320)-A (herein referred to as BCY32081); A-(SEQ ID NO: 321)-A (herein referred to as BCY32082); A-(SEQ ID NO: 322)-A (herein referred to as BCY32083); A-(SEQ ID NO: 323)-A (herein referred to as BCY32084); A-(SEQ ID NO: 324)-A (herein referred to as BCY32085); A-(SEQ ID NO: 325)-A (herein referred to as BCY32086); A-(SEQ ID NO: 326)-A (herein referred to as BCY32087); A-(SEQ ID NO: 327)-A (herein referred to as BCY32088); A-(SEQ ID NO: 328)-A (herein referred to as BCY32089); A-(SEQ ID NO: 329)-A (herein referred to as BCY32090); A-(SEQ ID NO: 330)-A (herein referred to as BCY32091); A-(SEQ ID NO: 331)-A (herein referred to as BCY32092); A-(SEQ ID NO: 332)-A (herein referred to as BCY32093); A-(SEQ ID NO: 333)-A (herein referred to as BCY32095); A-(SEQ ID NO: 334)-A (herein referred to as BCY32096); A-(SEQ ID NO: 335)-A (herein referred to as BCY32098); A-(SEQ ID NO: 336)-A (herein referred to as BCY32099); A-(SEQ ID NO: 337)-A (herein referred to as BCY32100); A-(SEQ ID NO: 338)-A (herein referred to as BCY32101); A-(SEQ ID NO: 339)-A (herein referred to as BCY32103); A-(SEQ ID NO: 340)-A (herein referred to as BCY32104); A-(SEQ ID NO: 341)-A (herein referred to as BCY32105); A-(SEQ ID NO: 342)-A (herein referred to as BCY32106); A-(SEQ ID NO: 343)-A (herein referred to as BCY32107); A-(SEQ ID NO: 344)-A (herein referred to as BCY32108); A-(SEQ ID NO: 345)-A (herein referred to as BCY32109);A-(SEQ ID NO: 346)-A (herein referred to as BCY32110); A-(SEQ ID NO: 347)-A (herein referred to as BCY32112); A-(SEQ ID NO: 348)-A (herein referred to as BCY32113); A-(SEQ ID NO: 349)-A (herein referred to as BCY32114); A-(SEQ ID NO: 350)-A (herein referred to as BCY32115); A-(SEQ ID NO: 351)-A (herein referred to as BCY32116); A-(SEQ ID NO: 352)-A (herein referred to as BCY32117); A-(SEQ ID NO: 353)-A (herein referred to as BCY32120); A-(SEQ ID NO: 354)-A (herein referred to as BCY32121); A-(SEQ ID NO: 355)-A (herein referred to as BCY32122); A-(SEQ ID NO: 356)-A (herein referred to as BCY32123); A-(SEQ ID NO: 357)-A (herein referred to as BCY32124); A-(SEQ ID NO: 358)-A (herein referred to as BCY32125); A-(SEQ ID NO: 359)-A (herein referred to as BCY19937); A-(SEQ ID NO: 360)-A (herein referred to as BCY19938); A-(SEQ ID NO: 361)-A (herein referred to as BCY19939); A-(SEQ ID NO: 362)-A (herein referred to as BCY19940); A-(SEQ ID NO: 363)-A (herein referred to as BCY19941); A-(SEQ ID NO: 364)-A (herein referred to as BCY19942); A-(SEQ ID NO: 365)-A (herein referred to as BCY19943); and A-(SEQ ID NO: 366)-A (herein referred to as BCY18253); or a modified derivative and / or pharmaceutically acceptable salt thereof.

10. A multimeric binding complex, or a pharmaceutically acceptable salt thereof, which comprises at least two bicyclic peptide ligands according to any one of claims 3 to 9, wherein said peptide ligands may be the same or different.

11. The multimeric binding complex, or a pharmaceutically acceptable salt thereof, according to claim 10 which comprises more than one bicyclic peptide which are the same (i.e. homomultimers).

12. The multimeric binding complex, or a pharmaceutically acceptable salt thereof, according to claim 10 which comprises bicyclic peptides which are different (i.e. heteromultimers).

13. The multimeric binding complex, or a pharmaceutically acceptable salt thereof, according to claim 10 which comprises two bicyclic peptides which are either the same (i.e. homodimers) or different (i.e. heterodimers), such as: BCY16282 AF488-AHDA-(amido-Peg10-triazolyl)[BCY15751]2 BCY26427 GTA-[amido-Peg10-triazolyl]2[BCY25826]2 BCY26435 GTA-[amido-Peg10-triazolyl]2[BCY24613]2 BCY28218 N-(Biotin-PEG23]-N-bis(PEG3-azide)[BCY24613]2 BCY28219 N-(Biotin-PEG23]-N-bis(PEG3-azide)[BCY21996]2 BCY28220 N-(Biotin-PEG23]-N-bis(PEG3-azide)[BCY25826]2 BCY28885 N-(Biotin-PEG23]-N-bis(PEG3-azide)[BCYBCY19741]2 BCY28887 N-(Biotin-PEG23]-N-bis(PEG3-azide)[BCY19743]2 BCY28222 N-(Biotin-PEG10)-N-bis(PEG10-azide)[BCY23767]2 BCY28223 N-(Biotin-PEG10)-N-bis(PEG10-azide)[BCY24613]2 BCY28224 N-(Biotin-PEG10)-N-bis(PEG10-azide)[BCY21996]2 BCY28225 N-(Biotin-PEG10)-N-bis(PEG10-azide)[BCY25826]2 BCY28886 N-(Biotin-PEG10)-N-bis(PEG10-azide)[BCY19741]2 BCY28888 N-(Biotin-PEG10)-N-bis(PEG10-azide)[BCY19743]2 BCY26436 GTA-[amido-Peg23-triazolyl]2[BCY24613]2 BCY31478 N-(amine-PEG10)-[BDP558-N3SC2]-N-bis(PEG10-azide)[BCY24613]2 BCY34406 N-(acid-PEG10)-[BDP558-N3SC1]-N-bis(PEG10-azide)[BCY24613]2 14. The multimeric binding complex, or a pharmaceutically acceptable salt thereof, according to claim 10 which comprises three bicyclic peptides which are either the same (i.e. homotrimers) or different (i.e. heterotrimers), such as wherein the heterotrimer comprises one bicyclic peptide of a first sequence and two bicyclic peptides of a second sequence, in particular: BCY25832 TCA-[amido-Peg10-triazolyl]3[BCY25826]3 BCY26437 TCA-[amido-Peg10-triazolyl]3[BCY24613]3 BCY28283 TCA-[amido-Peg5-triazolyl]3[BCY20840]3 BCY26442 TCA-[amido-Peg23-triazolyl]3[BCY24613]315. The multimeric binding complex, or a pharmaceutically acceptable salt thereof, according to claim 10 which comprises four bicyclic peptides which are either the same (i.e. homotetramers) or different (i.e. heterotetramers), such as wherein the heterotetramer comprises one bicyclic peptide of a first sequence and three bicyclic peptides of a second sequence, or wherein the heterotetramer comprises two bicyclic peptides of a first sequence and two bicyclic peptides of a second sequence, in particular: BCY15926 TET-[amido-Peg23-triazolyl]4[BCY15751]4 BCY25831 TET-[amido-Peg10-triazolyl]4[BCY25826]4 BCY26438 TET-[amido-Peg5-triazolyl]4[BCY24613]4 BCY26439 TET-[amido-Peg10-triazolyl]4[BCY24613]4 BCY21835 TET-[amido-Peg23-triazolyl]4[BCY20840]4 BCY21481 TET-[amido-Peg23-triazolyl]4[BCY19177]4 BCY21483 TET-[amido-Peg23-triazolyl]4[BCY21040]4 BCY29425 TET-[amido-Peg5-triazolyl]4[BCY23706]4 BCY29427 TET-[amido-Peg23-triazolyl]4[BCY23706]4 BCY28229 TET-[amido-Peg5-triazolyl]4[BCY21996]4 BCY28230 TET-[amido-Peg10-triazolyl]4[BCY21996]4 BCY26433 TET-[amido-Peg10-triazolyl]4[BCY23767]4 BCY26432 TET-[amido-Peg5-triazolyl]4[BCY23767]4 BCY28884 TET-[amido-Peg5-triazolyl]4[BCY19743]4 BCY30493 TET-[amido-Peg5-triazolyl]4[BCY28840]4 BCY30494 TET-[amido-Peg10-triazolyl]4[BCY28840]4 BCY30502 TET-[amido-Peg5-triazolyl]4[BCY28841]4 BCY30503 TET-[amido-Peg10-triazolyl]4[BCY28841]4 BCY30504 TET-[amido-Peg23-triazolyl]4[BCY28841]4 BCY26428 TET-[amido-Peg5-triazolyl]4[BCY25826]4 BCY25828 TET-[amido-Peg23-triazolyl]4[BCY25826]4 BCY26440 TET-[amido-Peg23-triazolyl]4[BCY24613]4 BCY26434 TET-[amido-Peg23-triazolyl]4[BCY23767]4 BCY29426 TET-[amido-Peg10-triazolyl]4[BCY23706]4 BCY28883 TET-[amido-Peg5-triazolyl]4[BCY19741]4 16. A pharmaceutical composition which comprises the peptide ligand according to claim 1, or bicyclic peptide ligand according to any one of claims 2 to 9, or multimeric binding complex according to any one of claims 10 to 15, or a pharmaceutically acceptable salt thereof, in combination with one or more pharmaceutically acceptable excipients.

17. The peptide ligand according to claim 1, or bicyclic peptide ligand according to any one of claims 2 to 9, or multimeric binding complex according to any one of claims 10 to 15, or a pharmaceutically acceptable salt thereof; or the pharmaceutical composition according to claim 16; for use in for use in preventing, suppressing or treating a disease or disorder mediated by TLR3.

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