aptamer

Abstract

The invention relates to aptamers, and to aptamers which are capable of binding specifically to protein biomarkers involved in neurodegenerative disorders. The invention also relates to the use of such aptamers in the diagnosis and / or prognosis of neurodegenerative disorders, such as Alzheimer's disease, and to methods of treating patients diagnosed or prognosed with a neurodegenerative disorder. The invention further provides biomarker detection methods, and apparatuses and kits for diagnosing and prognosing neurodegenerative disorders, for example a lateral flow test.

Description

[0001]Aptamer The invention relates to aptamers, and particularly, although not exclusively, to aptamers which are capable of binding specifically to protein biomarkers involved in neurodegenerative disorders. The invention also relates to the use of such aptamers in the diagnosis and / or prognosis of neurodegenerative disorders, such as Alzheimer’s disease, and to methods of treating patients diagnosed or prognosed with a neurodegenerative disorder. The invention further provides biomarker detection methods, and apparatuses and kits for diagnosing and prognosing neurodegenerative disorders, for example a lateral flow test. Neurodegenerative disorders, such as Alzheimer's disease (AD), Parkinson's disease, Huntington's disease or Motor Neurone disease, are some of the biggest socioeconomic burdens in the world with a growing worldwide incidence rate of almost 10 million new cases of dementia each year. Since both the incidence and prevalence of AD increases with age, the number of patients is growing significantly with an aging population. In 2015, there were over 46 million people living with dementia with an estimated socioeconomic cost of $800 billion annually and it is expected that the number of patients will rise to over 130 million by 2050 costing society over $2 trillion annually. AD was recently announced as the UK’s leading cause of death in the over 65’s, and in the US it is now the 6th leading cause of death across all ages. At present, there exists no single test that can be carried out to diagnose Alzheimer’s disease, or to prognose cognitive decline. Clinical classification of AD relies on a combination of subjective reporting, medical history evaluation, cognitive function tests, and costly brain imaging scans with no true classification possible until a post-mortem examination of the brain can be conducted. All of these tests require the involvement of expert medical practitioners, but are still of variable accuracy. They also take time, and are, therefore, slow and expensive. There is, therefore, a need to provide improved methods, apparatuses and / or kits for diagnosing disease in subjects suspected of having a neurodegenerative disorder, and especially Alzheimer’s disease, as well as for prognosing disease aetiology or progression in subjects already diagnosed with the condition. There is also a need to provide methods and apparatuses for screening, and detecting the risk of developing a neurodegenerative disorder in subjects who are pre- symptomatic for such conditions, or suspected of being so. Ideally, such improved methods and apparatuses are quick, quantitative (or at least semi-quantitative or qualitative), accurate, painless and cheap. The inventors have continued their previous research in this area and advanced the detection of acetylcholinesterase (AChE)-derived peptides. AChE is expressed at different stages of development in various forms, all of which have identical enzymatic activity, but which have very different molecular composition. The ‘tailed’ (T-AChE) is expressed at synapses and the inventors have previously identified two peptides that could be cleaved from the C-terminus, one referred to as “T14”, within the other which is known as “T30”, and which both have strong sequence homology to the comparable region of ^-amyloid. The AChE C-terminal peptide “T14”’ has been identified as being the salient part of the AChE molecule responsible for its range of non-hydrolytic actions. The synthetic 14 amino acids peptide analogue (i.e., “T14”), and subsequently the larger, more stable, and more potent amino acid sequence in which it is embedded (i.e., “T30”) display actions comparable to those reported for ‘non-cholinergic’ AChE, where the inert residue within the T30 sequence (i.e., “T15”) is without effect. As discussed in the Examples, the inventors have isolated novel aptamers which have been shown to bind specifically to the toxic peptides, “T14” and “T30”, and which can therefore be used to detect T14 and T30 in diagnostic or prognostic methods. Thus, the inventors believe that, in combination, these data form the basis for a first-in-class reliable diagnostic or prognostic screen for neurodegenerative disorders, as well as for diagnosing pre-symptomatic neurodegenerative disorders, such as early onset Alzheimer’s disease. Accordingly, in a first aspect of the invention, there is provided one or more aptamers capable of binding to: (i) a peptide comprising or consisting of SEQ ID No: 2 (T30), or a variant or fragment thereof, and / or (ii) a peptide comprising or consisting of SEQ ID No: 3 (T14), or a variant or fragment thereof. Advantageously, the aptamers described herein are shown to work effectively and provide a simple and quick means of testing the presence, absence or amount of T14 or T30 peptides in a sample using a simple gain-of signal assay format. In particular, the invention provides aptamers that are capable of specifically binding to the T14 or T30 peptides with unexpectedly high affinity and specificity. The aptamers described herein allow the amount of T14 or T30 peptides to be detected in biological fluids, such as nasal secretions. Following on from their previous studies, the inventors continued their research with acetylcholinesterase. Acetylcholinesterase is a serine protease that hydrolyses acetylcholine, and is well-known to the skilled person. The major form of acetylcholinesterase which is found in the brain is known as tailed acetylcholinesterase (T-AChE). The protein sequence of one embodiment of human tailed acetylcholinesterase (Gen Bank: AAA68151.1) is 614 amino acids in length, and is provided herein as SEQ ID No:1, as follows: 1 mrppqcllht pslaspllll llwllgggvg aegredaell vtvrggrlrg irlktpggpv 61 saflgipfae ppmgprrflp pepkqpwsgv vdattfqsvc yqyvdtlypg fegtemwnpn 121 relsedclyl nvwtpyprpt sptpvlvwiy gggfysgass ldvydgrflv qaertvlvsm 181 nyrvgafgfl alpgsreapg nvglldqrla lqwvqenvaa fggdptsvtl fgesagaasv 241 gmhllsppsr glfhravlqs gapngpwatv gmgearrrat qlahlvgcpp ggtggndtel 301 vaclrtrpaq vlvnhewhvl pqesvfrfsf vpvvdgdfls dtpealinag dfhglqvlvg 361 vvkdegsyfl vygapgfskd neslisraef lagvrvgvpq vsdlaaeavv lhytdwlhpe 421 dparlreals dvvgdhnvvc pvaqlagrla aqgarvyayv fehrastlsw plwmgvphgy 481 eiefifgipl dpsrnytaee kifaqrlmry wanfartgdp neprdpkapq wppytagaqq 541 yvsldlrple vrrglraqac afwnrflpkl lsatdtldea erqwkaefhr wssymvhwkn 601 qfdhyskqdr csdl [SEQ ID No:1] The amino acid sequence of T30 (which corresponds to the last 30 amino acid residues of SEQ ID No:1) is provided herein as SEQ ID No:2, as follows:- KAEFHRWSSYMVHWKNQFDHYSKQDRCSDL [SEQ ID No:2] Thus, preferably the one or more aptamers bind to T30 (SEQ ID No:2). The amino acid sequence of T14 (which corresponds to the 14 amino acid residues located towards the end of SEQ ID No:1, and lacks the final 15 amino acids found in T30) is provided herein as SEQ ID No:3, as follows:- AEFHRWSSYMVHWK [SEQ ID No:3] Thus, preferably the one or more aptamers bind to T14 (SEQ ID No:3). The amino acid sequence of T15 (which corresponds to the last 15 amino acid residues of SEQ ID No:1) is provided herein as SEQ ID No:4, as follows: NQFDHYSKQDRCSDL [SEQ ID No:4] In one embodiment, the one or more aptamers may bind to T15 (SEQ ID No:4). In another embodiment, however, the one or more aptamers may not bind to T15 (SEQ ID No:4). In an embodiment, one or more aptamers bind to T14 (SEQ ID No: 3) and none bind to T15 (SEQ ID No: 4). In yet another embodiment, one or more aptamers bind to T14 (SEQ ID No: 3), none bind to T15 (SEQ ID No: 4), and none bind to T30 (SEQ ID No: 2). In another embodiment, one or more aptamers bind to T30 (SEQ ID No: 2) and none bind to T15 (SEQ ID No: 4). In yet another embodiment, one or more aptamers bind to T30 (SEQ ID No: 2), none bind to T15 (SEQ ID No: 4), and none bind to T14 (SEQ ID No: 3). In an embodiment, one or more aptamers bind to T14 (SEQ ID No: 3) and one or more aptamers bind to the T15 region (SEQ ID No: 4) of T30 (SEQ ID No: 2). The aptamers described herein are small artificial ligands, comprising DNA, RNA or modifications thereof, capable of specifically binding to T14 or T30 peptides with high affinity and specificity. Typically, the aptamers of the invention are capable of specifically binding to a T14 region of the T30 peptide and / or the T15 region of the T30 peptide and / or a non-competing region of the T14 region of the T30 peptide. As used herein, “aptamer”, “nucleic acid molecule” or “oligonucleotide” are used interchangeably to refer to a non-naturally occurring nucleic acid molecule that has a desirable action on a target molecule (i.e., T14 or T30 peptides). The aptamers of the invention may be DNA aptamers. For example, the aptamers may be formed from single-stranded DNA (ssDNA). Alternatively, the aptamers of the invention may be RNA aptamers. For example, the aptamers can be formed from single-stranded RNA (ssRNA). The aptamers of the invention may comprise modified nucleic acids as described herein. In preferred embodiments, the aptamers of the invention are DNA aptamers (e.g. ssDNA aptamers). The aptamers of the invention may be at least 15 nucleotides long. Preferably, the aptamers are at least 30 nucleotides long, or at least 40 nucleotides long, or at least 50 nucleotides long. Preferably, the aptamers are at least 60 nucleotides long, or at least 70 nucleotides long, or at least 80 nucleotides long. The aptamers of the invention may be less than 120 nucleotides long. Preferably, the aptamers are less than 110 nucleotides long, or less than 100 nucleotides long, or less than 90 nucleotides long. SEQ ID No’s 5-17 below are preferred aptamers which were isolated against the T14 peptide. It will be appreciated therefore that SEQ ID No’s 5-17 are preferred aptamers which have a preference for binding to the T14 peptide. SEQ ID NO: 5 shows the full nucleic acid sequence of T14 Aptamer (T14_7R_T2): CCAGTGTAGACTACTCAATGCGTGGACTGGTCGGGTTTGGATTCGGCAGATGAATCAGTAGTACTATCCACAGGTCAA CC [SEQ ID No: 5] SEQ ID NO: 6 shows the full nucleic acid sequence of T14 Aptamer (T14_7R_T3): CCAGTGTAGACTACTCAATGCCGTGGACTGGTCGGGTTGGATTCGGCAGATGAATCAGTAGTACTATCCACAGGTCAA CC [SEQ ID No: 6] SEQ ID NO: 7 shows the full nucleic acid sequence of T14 Aptamer (T14_7R_T4): CCAGTGTAGACTACTCAATGCCGTGGACTGGTCGGGCTTGGATTCGGCAGATGAATCAGTAGTACTATCCACAGGTCA ACC [SEQ ID No: 7] SEQ ID NO: 8 shows the full nucleic acid sequence of T14 Aptamer (T14_7R_T5): CCAGTGTAGACTACTCAATGCCGTGGACTGGTCGGGGTTTGGATTCGGCAGATGAATCAGTAGTACTATCCACAGGTC AACC [SEQ ID No: 8] SEQ ID NO: 9 shows the full nucleic acid sequence of T14 Aptamer (T14_7R_T6): CCAGTGTAGACTACTCAATGCCGTGGACTGGTCGGGTTTGGACTCGGCAGATGAATCAGTAGTACTATCCACAGGTCA ACC [SEQ ID No: 9] SEQ ID NO: 10 shows the full nucleic acid sequence of T14 Aptamer (T14_7R_Cluster2_T1_LED_2): CCAGTGTAGACTACTCAATGCTAGGTGTGGTGACCTTGAGCTGCGGATCGGAGGGAGGGTGGGGTACTATCCACAGGT CAACC [SEQ ID No: 10] SEQ ID NO: 11 shows the full nucleic acid sequence of T14 Aptamer (T14_5R_Cluster8_T1_LED_2): CCAGTGTAGACTACTCAATGCCGTGGACTGGTCGGGTTTGGATTCGGCAGATGAGTCAGTAGTACTATCCACAGGTCA ACC [SEQ ID No: 11] SEQ ID NO: 12 shows the full nucleic acid sequence of T14 Aptamer (T14_7R_T7): CCAGTGTAGACTACTCAATGCCGTGGACTGGTCGGGTTTGGATCGGCAGATGAATCAGTAGTACTATCCACAGGTCAA CC [SEQ ID No: 12] SEQ ID NO: 13 shows the full nucleic acid sequence of T14 Aptamer (T14_7R_T8): CCAGTGTAGACTACTCAATGCCGTGGACTGGTCGGGTTTGGATTCGGCAGATGAATCAGAGTACTATCCACAGGTCAA CC [SEQ ID No: 13] SEQ ID NO: 14 shows the full nucleic acid sequence of T14 Aptamer (T14_7R_T9): CCAGTGTAGACTACTCAATGCCGTGGACTGGTCGGGTTTTGGATTCGGCAGATGAATCAGTAGTACTATCCACAGGTC AACC [SEQ ID No: 14] SEQ ID NO: 15 shows the full nucleic acid sequence of T14 Aptamer (T14_7R_T10): CCAGTGTAGACTACTCAATGCCGTGGACTGGTCGGGTTTGGATTCGGCAGATGGATCAGTAGTACTATCCACAGGTCA ACC [SEQ ID No: 15] SEQ ID NO: 16 shows the full nucleic acid sequence of T14 Aptamer (T14_7R_Cluster5_T1_LED_1): CCAGTGTAGACTACTCAATGCCGTGGACTGGTCGGGGTTTTGGATTCGGCAGATGAATCAGTAGTACTATCCACAGGT CAACC [SEQ ID No: 16] SEQ ID NO: 17 shows the full nucleic acid sequence of T14 Aptamer (T14_3S_Cluster6_T1_LED_1): CCAGTGTAGACTACTCAATGCAGTCATACCTTACCTTTACTGCGTCATTCTTTTTCATATCGTACTATCCACAGGTCA ACC [SEQ ID No: 17] SEQ ID No’s 18-34 below are preferred aptamers which were isolated against the T30 peptide. It will therefore be appreciated that SEQ ID No’s 18-34 are preferred aptamers which have a preference for binding to the T30 peptide. SEQ ID NO: 18 shows the full nucleic acid sequence of T30 Aptamer (T30_7R_T1): CCAGTGTAGACTACTCAATGCTGGTGTGGTGACCTTGAGCTGCGGATCGGAGGGAGGGTGGGTACTATCCACAGGTCA ACC [SEQ ID No: 18] SEQ ID NO: 19 shows the full nucleic acid sequence of T30 Aptamer (T30_9R_Cluster11_1_LED_2): CAGTGTAGACTACTCAATGCTAGGTGTGGTGACCTTGAGCTGCGGATCGGAGGGGAGGGGTGGGTACTATCCACAGGT CAACC [SEQ ID No: 19] SEQ ID NO: 20 shows the full nucleic acid sequence of T30 Aptamer (T30_9R_Cluster19_1_LED_2): CCAGTGTAGACTACTCAATGCTAGGTGTGGTGACCTTGAGCTGCGGATCGGAGGAGGTGGTACTATCCACAGGTCAAC C [SEQ ID No: 20] SEQ ID NO: 21 shows the full nucleic acid sequence of T30 Aptamer (T30_9R_Cluster1_6_LED_1): CCAGTGTAGACTACTCAATGCTAGGTGTGGTGACCTTGAGCTGCGGATCGGAGGGGAGGGTGGGTACTATCCACAGGT CAACC [SEQ ID No: 21] SEQ ID NO: 22 shows the full nucleic acid sequence of T30 Aptamer (T30_9R_T1): CCAGTGTAGACTACTCAATGCTAGGTGTGGTGACCTTGAGCTGCGGATCGGAGGGAGGTGGGTACTATCCACAGGTCA ACC [SEQ ID No: 22] SEQ ID NO: 23 shows the full nucleic acid sequence of T30 Aptamer (T30_9R_Cluster5_3_LED_1): CCAGTGTAGACTACTCAATGCACACCAACCTCTTGAGTCCTTGCTTCTCGCCGCCCCCTAGTACTATCCACAGGTCAA CC [SEQ ID No: 23] SEQ ID NO: 24 shows the full nucleic acid sequence of T30 Aptamer (T30_9R_Cluster1_10_LED_1): CCAGTGTAGACTACTCAATGCTAGTGTGGTGACCTTGAGCTGCGGATCGGAGGGAGGGTGGGTACTATCCACAGGTCA ACC [SEQ ID No: 24] SEQ ID NO: 25 shows the full nucleic acid sequence of T30 Aptamer (T30_7R_Cluster2_3_LED_1): CCAGTGTAGACTACTCAATGCTCTATTCCGTATAGTACGTTAGGTTGGGTAGGTTGGTACGTACTATCCACAGGTCAA CC [SEQ ID No: 25] SEQ ID NO: 26 shows the full nucleic acid sequence of T30 Aptamer (T30_7R_Cluster2_4_LED_1): CCAGTGTAGACTACTCAATGCTCCTATTCCGTATAGTACGTTAGGTTGGGGTAGGTTGGTACGTACTATCCACAGGTC AACC [SEQ ID No: 26] SEQ ID NO: 27 shows the full nucleic acid sequence of T30 Aptamer (T30_7R_Cluster6_1_LED_2): CCAGTGTAGACTACTCAATGCTAGGTGTGGTGACCTTGAGCTGCGGATCGGAGGAGGTGGGTACTATCCACAGGTCAA CC [SEQ ID No: 27] SEQ ID NO: 28 shows the full nucleic acid sequence of T30 Aptamer (T30_7R_Cluster6_2_LED_1): CCAGTGTAGACTACTCAATGCTAGGTGTGGTGACCTTGAGCTGCGGATGCGGAGGAGGTGGGTACTATCCACAGGTCA ACC [SEQ ID No: 28] SEQ ID NO: 29 shows the full nucleic acid sequence of T30 Aptamer (T30_9R_Cluster11_1_LED_1): CAGTGTAGACTACTCAATGCTAGGTGTGGTGACCTTGAGCTGCGGATCGGAGGGGAGGGGTGGGTACTATCCACAGGT CAACC [SEQ ID No: 29] SEQ ID NO: 30 shows the full nucleic acid sequence of T30 Aptamer (T30_9R_Cluster17_1_LED_1): CCAGTGTAGACTACTCAATGCTAGGTGTGGTGACCTTGAGCTGCGGATCGGAGGGAGGGGTGGGTACTATCCACAGGT CAACC [SEQ ID No: 30] SEQ ID NO: 31 shows the full nucleic acid sequence of T30 Aptamer (T30_9R_Cluster19_1_LED_1): CCAGTGTAGACTACTCAATGCTAGGTGTGGTGACCTTGAGCTGCGGATGCGGAGGAGGGTGGGTACTATCCACAGGTC AACC [SEQ ID No: 31] SEQ ID NO: 32 shows the full nucleic acid sequence of T30 Aptamer (T30_2S_T5): CCAGTGTAGACTACTCAATGCTGAAGGGCCGCCCCATTCCCTATATACATTCGTCCATCTTGTACTATCCACAGGTCA ACC [SEQ ID No: 32] SEQ ID NO: 33 shows the full nucleic acid sequence of T30 Aptamer (T30_2S_T6): CCAGTGTAGACTACTCAATGCTCACCTTCTCGACTCCTTTATGCAGTGTCCAGCCGTAAAAGTACTATCCACAGGTCA ACC [SEQ ID No: 33] SEQ ID NO: 34 shows the full nucleic acid sequence of T30 Aptamer (T30_2S_T8): CCAGTGTAGACTACTCAATGCTGCGGATTCCCTCCGCAATTTAACCCACTCTGTCATTCATGTACTATCCACAGGTCA ACC [SEQ ID No: 34] Accordingly, the one or more aptamers may comprise: (a) a nucleic acid sequence selected from any one or more of SEQ ID NOs: 5- 34; (b) a nucleic acid sequence having at least about 85%, 90%, 95% or 99% sequence identity or more with any one or more of the sequences of (a); or (c) a nucleic acid sequence having at least about 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75 or more consecutive nucleotides of any one or more of the sequences of (a) or (b). In certain embodiments, the one or more aptamers of the invention are capable of binding to the T14 region of the peptide and comprise: (a) a nucleic acid sequence selected from any one or more of SEQ ID NOs: 5- 17; (b) a nucleic acid sequence having at least about 85%, 90%, 95% or 99% sequence identity or more with any one or more of the sequences of (a); or (c) a nucleic acid sequence having at least about 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75 or more consecutive nucleotides of any one or more of the sequences of (a) or (b). In certain embodiments, the one or more aptamers of the invention are capable of binding to the T30 region of the peptide and comprise: (a) a nucleic acid sequence selected from any one or more of SEQ ID NOs: 18- 34; (b) a nucleic acid sequence having at least about 85%, 90%, 95% or 99% sequence identity or more with any one or more of the sequences of (a); or (c) a nucleic acid sequence having at least about 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75 or more consecutive nucleotides of any one or more of the sequences of (a) or (b). Such aptamers as shown as SEQ ID No: 5-34 are capable of unexpectedly high affinity binding to an accessible region of the T14 or T30 peptides. Such aptamers are advantageously capable of binding to T14 or T30 peptides present in a nasal swab sample. As described herein, these exhibit an unexpected wide range of advantageous properties and have also shown to be particularly effective in an ELISA-like format or a Lateral Flow Test format. As described herein, the aptamers set forth in SEQ ID NOs: 5-17 (or fragments or variants thereof) are capable of high affinity binding to the T14 region of the T30 peptide. Advantageously, such aptamers may be used in combination with the T15 or other T30 binding aptamers (or variants thereof) as described herein in sandwich assay platforms (e.g. ELISA-like assays or Lateral Flow Tests). As described herein, the aptamers set forth in SEQ ID NOs: 18-34 (or fragments or variants thereof) are capable of high affinity binding to the T30 peptide. In certain embodiments, the aptamers of the invention comprise or consist of a nucleic acid sequence selected from any one of SEQ ID NOs: 5-34, or fragments thereof. The aptamers of the invention may comprise natural or non-natural nucleotides and / or base derivatives (or combinations thereof). In certain embodiments, the aptamers comprise one or more modifications such that they comprise a chemical structure other than deoxyribose, ribose, phosphate, adenine (A), guanine (G), cytosine (C), thymine (T), or uracil (U). The aptamers may be modified at the nucleobase, at the sugar or at the phosphate backbone. In certain embodiments, the aptamers comprise one or more modified nucleotides. Exemplary modifications include for example nucleotides comprising an alkylation, arylation or acetylation, alkoxylation, halogenation, amino group, or another functional group. Examples of modified nucleotides include 2'-fluoro ribonucleotides, 2'-NH2 -, 2'-OCH3 - and 2'-O-methoxyethyl ribonucleotides, which are used for RNA aptamers. The aptamers of the invention may be wholly or partly phosphorothioate or DNA, phosphorodithioate or DNA, phosphoroselenoate or DNA, phosphorodiselenoate or DNA, locked nucleic acid (LNA), peptide nucleic acid (PNA), N3'-P5 'phosphoramidate RNA / DNA, cyclohexene nucleic acid (CeNA), tricyclo DNA (tcDNA) or spiegelmer, or the phosphoramidate morpholine (PMO) components or any other modification known to those skilled in the art (see also Chan et al., Clinical and Experimental Pharmacology and Physiology (2006) 33, 533-540). Some of the modifications allow the aptamers to be stabilized against nucleic acid- cleaving enzymes. In the stabilization of the aptamers, a distinction can generally be made between the subsequent modification of the aptamers and the selection with already modified RNA / DNA. The stabilization does not necessarily affect the affinity of the modified RNA / DNA aptamers but prevents the rapid decomposition of the aptamers in an organism or biological solutions by RNases / DNases. An aptamer is referred to as stabilized in the context of the present invention if the half-life in the sample (e.g. biological medium) is greater than one minute, preferably greater than one hour, more preferably greater than one day. The aptamers may also be modified with reporter molecules which, in addition to the detection of the labelled aptamers, may also contribute to increasing the stability. Aptamers are characterised by the formation of a specific three-dimensional structure that depends on the nucleic acid sequence. The three-dimensional structure of an aptamer arises due to Watson and Crick intramolecular base pairing, Hoogsteen base pairing (quadruplex), wobble-pair formation or other non-canonical base interactions. This structure enables aptamers, analogous to antigen-antibody binding, to bind target structures accurately. A nucleic acid sequence of an aptamer may, under defined conditions, have a three-dimensional structure that is specific to a defined target structure. As used herein, the term "antigen" refers to a molecular target of an aptamer (e.g. T14 or T30), which is expressed in a tissue, a cell or a virus and / or secreted in body fluids such as urine, saliva, nasal swab, sputum, tear, blood, seminal and cerebrospinal fluids. In certain embodiments, the aptamers of the invention comprise or consist of a nucleic acid sequence selected from any one of SEQ ID NOs 5 to 17 (i.e., aptamers generated against the T14 region of the T30 peptide). In certain embodiments, the aptamers of the invention comprise or consist of any one of SEQ ID NOs 5 to 17 (or fragments or variants thereof). As described further herein, these aptamers are capable of binding to an accessible region of the T14 peptide within the T30 peptide (i.e., capable of binding to the T14 region in its native conformation as part of the T30 peptide). In certain embodiments, the aptamers of the invention comprise or consist of any one of SEQ ID NOs 5-17 (or fragments or variants thereof). As described further herein, these aptamers specifically bind to T14 peptides in a nasal swab sample. In certain embodiments, the aptamers of the invention comprise or consist of a nucleic acid sequence selected from any one of SEQ ID NOs 18 to 34 (i.e., aptamers generated against the T30 peptide, but not specifically directed to the T14 region thereof). In certain embodiments, the aptamers of the invention comprise or consist of any one of SEQ ID NOs 18 to 34 (or fragments or variants thereof). As described further herein, these aptamers are capable of binding to an accessible region of the T30 peptide (i.e., capable of binding to the T30 peptide in its native conformation). In certain embodiments, the aptamers of the invention comprise or consist of any one of SEQ ID NOs 18-34 (or fragments or variants thereof). As described further herein, these aptamers specifically bind to T30 peptides in a nasal swab sample. As used herein, “sequence identity” refers to the percentage nucleotide identity (or homology) over the entire length of the defined sequence (SEQ ID NO). The sequence identity is calculated based on the percentage of nucleotides in a candidate sequence that are identical with the nucleotides in said sequences after aligning the sequences and introducing gaps, if necessary, to achieve the maximum percent sequence identity. Alignment for purposes of determining percent nucleic acid sequence identity can be achieved in various ways that are within the skill in the art, for instance, using publicly available computer software such as BLAST, BLAST-2, ALIGN, CLUSTALW or MegAlign (DNASTAR) software. For example, % nucleic acid sequence identity values can be generated using sequence comparison computer programs found on the European Bioinformatics Institute website (http: / / www.ebi.ac.uk). With respect to any protein sequences, “sequence identity” also refers to the percentage amino acid identity (or homology) over the entire length of the defined sequence. The sequence identify is calculated based on the percentage of amino acid residues in a sequence that are identical with the amino acid residues in said sequences after aligning the sequences and introducing gaps, if necessary, to achieve the maximum percent sequence identity. Alignment for purposes of determining percent amino acid sequence identity can be achieved in various ways that are within the skill in the art, for instance, using publicly available computer software such as BLASTP. In certain embodiments, aptamers of the invention comprise or consist of a minimal effective fragment of any one of the sequences as described herein. For example, the aptamers may comprise or consist of a minimal effect fragment of any one of SEQ ID NOs 5-34. Herein, a “minimal effective fragment” is understood to mean a fragment (e.g. portion) of the full-length aptamer capable of binding to T14 or T30 peptides with at least the same (or improved) specificity and / or affinity as compared to the full- length aptamer. A minimal effective fragment may compete for binding to T14 or T30 peptides with the full-length aptamer. As used herein, the term “high affinity” is understood to mean, for example, an aptamer that binds to the protein with a binding dissociation equilibrium constant (KD) of less than about 100 nM, less than about 90nM, less than about 80nM, less than about 70nM, less than about 60nM, less than about 50nM, less than about 40nM, less than about 30nM, less than about 20nM, less than about 10nM, less than about 5nM, less than about 1nM, less than about 0.9nM, less than about 0.8nM, less than about 0.7nM, less than about 0.6nM, less than about 0.5nM, less than about 0.4nM, less than about 0.3nM, less than about 0.2nM, less than about 0.1nM, less than about 90 pM, less than about 80 pM, less than about 70 pM, less than about 60 pM, less than about 50 pM, less than about 40 pM, less than about 30 pM, less than about 20 pM, less than about 10 pM, less than about 5 pM, less than about 4 pM, less than about 3 pM, less than about 2 pM, less than about 1 pM or less. As used herein, the term “low affinity” is understood to mean, for example, an aptamer that binds to the protein with a binding dissociation equilibrium constant (KD) of more than about 1 µM, more than about 2 µM, more than about 3 µM, more than about 4 µM, more than about 5 µM, more than about 6 µM, more than about 7 µM, more than about 8 µM, more than about 9 µM, more than about 10 µM or has no detectable response. The binding affinity of aptamers may be measured by any method known to a person skilled in the art, including, for example, surface plasmon resonance (SPR), Biolayer Interferometry (BLI), ELISA, fluorescence assays such as fluorescence anisotropy or fluorescence polarisation, Microscale Thermophoresis or the like. As described herein, such aptamer pairs are particularly useful in sandwich assays or the like. In alternative embodiments (e.g., biosensor applications etc.) any one aptamer as described herein may be used. Thus, in certain embodiments, the invention provides a single aptamer. However, in other embodiments, the invention provides more than one aptamer, e.g. two, three, four, five or more aptamers. In certain embodiments, the invention provides two or more aptamers (e.g. aptamer pair, triplet or more) that bind to two or more different regions of the T14 or T30 peptides as described herein. In other words, the two or more aptamers do not compete for binding to the same epitope of the T14 or T30 peptides. Thus, in certain embodiments, the invention provides two or more aptamers (e.g. two, three, four, five or more aptamers) capable of binding to two or more (e.g. two, three, four, five or more) different regions of the T14 or T30 peptides as described herein. For example, the invention provides two or more aptamers comprising any first aptamer as described herein that is capable of binding to a first region of the T30 peptide and any second aptamer as described herein that binds to a different or non-competing region of the T30 peptide. In other words, the two or more aptamers do not compete for binding to the same epitope of the T30 peptide. In certain embodiments, the invention provides two or more aptamers, wherein a first aptamer is capable of binding to the T14 or T30 peptides and a second aptamer is capable of binding to either a different (non-overlapping) region of the T14 or T30 peptides or to the T15 region of the T30 peptide. In certain embodiments, the invention provides two or more aptamers for use in a two-site binding assay (e.g. sandwich assay). Exemplary sandwich assays include, but are not limited to, ELISA, lateral flow assays and many other assays known to one skilled in the art. Such assays may utilise compatible pairs of aptamers capable of binding to different regions (e.g. epitopes) and / or regions of the T14 or T30 peptides as described herein. In other words, the binding of one aptamer (of a compatible pair) to the T14 or T30 peptides may not interfere with (or affect) the binding of the second aptamer (of the compatible pair) to the equivalent peptide. In certain embodiments, the invention provides at least a pair of aptamers comprising: (a) a first aptamer comprising a nucleic sequence selected from any one of SEQ ID NOs 5-34, or a sequence having at least about 85%, 90%, 95% or 99% sequence identity or more with any one of SEQ ID NOs 5-34; and (b) a second aptamer comprising a nucleic sequence selected from any one of SEQ ID NOs 5-34, or a sequence having at least about 85%, 90%, 95% or 99% sequence identity or more with any one of SEQ ID NOs 5-34. In certain embodiments, the invention provides two or more aptamers (e.g. a compatible pair, triplet, or more) selected from any two or more nucleic acids selected from: - SEQ ID NOs 5-17 (or variants thereof); and / or - SEQ ID NOs 18-34 (or variants thereof). In certain embodiments, the invention provides two or more aptamers (e.g. a compatible pair, triplet, or more) selected from any two or more nucleic acids selected from any one of SEQ ID NOs 5-34 (or variants thereof) and any other one of SEQ ID NOs 5-34 (or variants thereof). In preferred embodiments, the invention provides at least two or more aptamers (e.g. aptamer pair, triplet or more) wherein at least one aptamer is capable of binding to the T14 and at least one aptamer is capable of binding to the T15 region or a non-competing region of the T14 region of the T30 peptide as described herein. In certain embodiments, the aptamer against the T14 region may be used for “capture”, whilst the aptamer against the T15 region, or non-competing T14 region may be used for “detection” as further described herein. Alternatively, the aptamer against the T15 region, or non-competing T14 region may be used for “capture”, whilst the aptamer against the T14 region may be used for “detection” as further described herein. As described herein, a “first aptamer” of the invention may be used for capture or detection. If the first aptamer is used for capture, the “second aptamer” may be used for detection. If the first aptamer is used for detection, the second aptamer may be used for capture. Such aptamers are particularly suitable for use in sandwich assays as described herein. In certain embodiments, the one or more aptamers are isolated. In certain embodiments, the one or more aptamers are DNA aptamers. In certain embodiments, the aptamers of the invention are used to detect and / or quantify the amount of T14 or T30 peptides in a sample. Typically, the aptamers comprise a detectable label or detectable molecule. In certain embodiments, the one or more aptamers comprise a detectable label or detectable molecule to form a complex. Hence, in a second aspect, the invention provides a complex comprising any one or more aptamers according to the first aspect, and a detectable molecule. Any label capable of facilitating detection and / or quantification of the aptamers may be used herein. In certain embodiments, the detectable label is a fluorescent moiety, e.g. a fluorescent / quencher compound. Fluorescent / quencher compounds are known in the art. See, for example, Mary Katherine Johansson, Methods in Molecular Biol. 335: Fluorescent Energy Transfer Nucleic Acid Probes: Designs and Protocols, 2006, Didenko, ed., Humana Press, Totowa, NJ, and Marras et al., 2002, Nucl. Acids Res. 30, el22 (incorporated by reference herein). In certain embodiments, the detectable label is FAM. In certain embodiments, the FAM-label is situated at the first or second primer region of the aptamer. The person skilled in the art would understand that the label could be located at any suitable position within the aptamer. Moieties that result in an increase in detectable signal when in proximity of each other may also be used herein, for example, as a result of fluorescence resonance energy transfer ("FRET"); suitable pairs include but are not limited to fluoroscein and tetramethylrhodamine; rhodamine 6G and malachite green, and FITC and thiosemicarbazole, to name a few. In certain embodiments, the detectable label is selected from a fluorophore, a nanoparticle, a quantum dot, an enzyme, a radioactive isotope, a pre-defined sequence portion, a biotin, a desthiobiotin, a thiol group, an amine group, an azide, an aminoallyl group, a digoxigenin, an antibody, a catalyst, a colloidal metallic particle, a colloidal non-metallic particle, an organic polymer, a latex particle, a nanofiber, a nanotube, a dendrimer, a protein, and a liposome. In an embodiment, the detectable label is biotin. In one embodiment, therefore, the invention provides one or more aptamers that may be biotinylated. It will be appreciated that the term “biotinylated” can mean that biotin is attached to a protein or other macromolecule. As such, it will be appreciated that the phrase “aptamers that are biotinylated” can mean aptamers that are attached to biotin. In one embodiment, therefore, the invention provides one or more biotinylated aptamer capable of binding to: (i) a peptide comprising or consisting of SEQ ID No: 2 (T30), or a variant or fragment thereof, and / or (ii) a peptide comprising or consisting of SEQ ID No:3 (T14), or a variant or fragment thereof. In certain embodiments, the detectable label is a fluorescent protein such as Green Fluorescent Protein (GFP) or any other fluorescent protein known to those skilled in the art. In certain embodiments, the detectable label is an enzyme. For example, the enzyme may be selected from horseradish peroxidase, alkaline phosphatase, urease, β-galactosidase or any other enzyme known to those skilled in the art. In certain embodiments, the nature of the detection will be dependent on the detectable label used. For example, the label may be detectable by virtue of its colour e.g. gold nanoparticles. A colour can be detected quantitatively by an optical reader or camera e.g. a camera with imaging software. In certain embodiments, the detectable label is a fluorescent label e.g. a quantum dot. In such embodiments, the detection means may comprise a fluorescent plate reader, strip reader or similar, which is configured to record fluorescence intensity. In embodiments in which the detectable label is an enzyme label, the detection means may, for example, be colorimetric, chemiluminescence and / or electrochemical (for example, using an electrochemical detector). Typically, electrochemical sensing is through conjugation of a redox reporter (e.g. methylene blue or ferrocene) to one end of the aptamer and a sensor surface to the other end. Typically, a change in aptamer conformation upon target binding changes the distance between the reporter and sensor to provide a readout. In certain embodiments, the detectable label may further comprise enzymes such as horseradish peroxidase (HRP), Alkaline phosphatase (APP) or similar, to catalytically turnover a substrate to give an amplified signal. In certain embodiments, the invention provides a complex (e.g. conjugate) comprising aptamers of the invention and a detectable molecule. Typically, the aptamers of the invention are covalently or physically conjugated to a detectable molecule. In certain embodiments, the detectable molecule is a visual, optical, photonic, electronic, acoustic, opto-acoustic, mass, electrochemical, electro-optical, spectrometric, enzymatic, or otherwise physically, chemically or biochemically detectable label. In certain embodiments, the detectable molecule is detected by luminescence, UV / VIS spectroscopy, enzymatically, electrochemically or radioactively. Luminescence refers to the emission of light. For example, photoluminescence, chemiluminescence and bioluminescence are used for detection of the label. In photoluminescence or fluorescence, excitation occurs by absorption of photons. Exemplary fluorophores include, without limitation, bisbenzimidazole, fluorescein, acridine orange, Cy5, Cy3 or propidium iodide, tetramethyl-6-carboxyhodamine (TAMRA), Texas Red (TR), rhodamine, Alexa Fluor dyes (et al. Fluorescent dyes of different wavelengths from different companies), quantum dots or other related semiconductor particles; which can be covalently coupled to aptamers. In certain embodiments, the detectable molecule is a non-fluorescent particle e.g. gold nanoparticle, colloidal non-metallic particle, organic polymer, latex particle, nanofiber (e.g. carbon nanofiber), nanotube (e.g. carbon nanotube), dendrimer, protein or liposome with signal-generating substances. Colloidal particles can be detected colorimetrically. In certain embodiments, the detectable molecule is an enzyme. In certain embodiments, the enzyme may convert substrates to coloured products, e.g. peroxidase, luciferase, β-galactosidase or alkaline phosphatase. For example, the colourless substrate X-gal is converted by the activity of β-galactosidase to a blue product whose colour is visually detected. In certain embodiments, the detection molecule is a radioactive isotope. The detection can also be carried out by means of radioactive isotopes with which the aptamer is labelled, including but not limited to 3H, 14C, 32P, 33P, 35S or 125I, more preferably 32P, 33P or 125I. In the scintillation counting, the radioactive radiation emitted by the radioactively labelled aptamer target complex is measured indirectly. A scintillator substance is excited by the isotope’s radioactive emissions. During the transition of the scintillation material, back to the ground state, the excitation energy is released again as flashes of light, which are amplified and counted by a photomultiplier. In certain embodiments, the detectable molecule is selected from digoxigenin and biotin. Thus, the aptamers may also be labelled with digoxigenin or biotin, which are bound for example by antibodies or streptavidin, which may in turn carry a label, such as an enzyme conjugate. The prior covalent linkage (conjugation) of an aptamer with an enzyme can be accomplished in several known ways. Detection of aptamer binding may also be achieved through labelling of the aptamer with a radioisotope in an RIA (radioactive immunoassay), preferably with 125I, or by fluorescence in a FIA (fluoroimmunoassay) with fluorophores, preferably with fluorescein or FITC. In certain embodiments, the one or more aptamers of the invention further comprise one or more linker sequences. For example, the linker sequence may comprise a nucleic acid sequence which is configured to hybridise to at least a portion of the aptamer. The linker sequence may be configured to form a double- stranded duplex structure with at least a portion of the aptamer of the invention. In certain embodiments, the linker sequence is between about 10 to about 20 nucleotides in length, e.g. about 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more nucleotides in length. Typically, the linker sequence is complementary to the aptamer over at least a portion of its length. In certain embodiments, the linker sequence comprises a suitable functional moiety to allow surface attachment to the aptamer. The functional moiety may be selected from biotin, thiol, and amine or any other suitable group known to those skilled in the art. In certain embodiments, the linker sequence or aptamer comprises a spacer molecule e.g. a spacer molecule selected from a polynucleotide molecule, C6 spacer molecule, a C12 spacer molecule, another length C spacer molecule, a hexaethylene glycol molecule, a hexanediol, and / or polyethylene glycol. The linker may be for example a biotin linker. In certain embodiments, the linker sequence or aptamer may be conjugated to streptavidin, avidin and / or neutravidin. In certain embodiments, the linker sequence or aptamer may be modified for attachment to the support surface. For example, the linker sequence or aptamer may be attached via a silane linkage. The linker sequence or aptamer may be succinylated (e.g. to attach the linker sequence or aptamer to aminophenyl or aminopropyl-derivatized glass). Aptly, the support is aminophenyl or aminopropyl- derivatized. In certain embodiments, the linker sequence or aptamer comprises a NH2 modification (e.g. to attach to epoxy silane or isothiocyanate coated glass). Typically, the support surface is coated with an epoxy silane or isothiocyanate. In certain embodiments, the linker sequence or aptamer is hydrazide-modified in order to attach to an aldehyde or epoxide molecule. Aptamers of the invention may be immobilised to a support via one or more linker sequences as described herein. In certain embodiments, therefore, the aptamer or linker sequence is attached to a support. Typically, the support is a solid support such as a wafer, slide, plate, membrane or a bead. The support may be a two-dimensional support e.g. a microplate or a three-dimensional support e.g. a bead. In certain embodiments, the support may comprise at least one or more silica wafers, fibres, magnetic beads etc. In certain embodiments, the solid support is part of a swab that is derivatised with one or more aptamers of the invention. In certain embodiments, the support may comprise at least one nanoparticle e.g. gold nanoparticles or the like. In yet further embodiments, the support comprises a microtiter or other assay plate, a strip, a membrane, a film, a gel, a chip, a microparticle, a nanofiber, a nanotube, a micelle, a micropore, a nanopore, a silica - fibre or similar substrate forming a swab or a biosensor surface. In certain embodiments, the biosensor surface may be a probe tip surface, a biosensor flow- channel or similar. In certain embodiments, the aptamer or linker sequence may be attached, directly or indirectly, to a magnetic bead, which may be e.g. carboxy-terminated, avidin- modified or epoxy-activated or otherwise modified with a compatible reactive group. Immobilisation of oligonucleotides to a support e.g. a solid phase support can be accomplished in a variety of ways and in any manner known to those skilled in the art for immobilising DNA or RNA on solids. The immobilisation of aptamers on nanoparticles is e.g. as described in WO2005 / 13817. For example, a solid phase of paper or a porous material may be wetted with the liquid phase aptamer, and the liquid phase subsequently volatilized leaving the aptamer in the paper or porous material. In certain embodiments, the support comprises a membrane, e.g. a nitrocellulose, a polyethylene (PE), a polytetrafluoroethylene (PTFE), a polypropylene (PP), a cellulose acetate (CA), a polyacrylonitrile (PAN), a polyimide (PI), a polysulfone (PS), a polyethersulfone (PES) membrane or an inorganic membrane comprising aluminium oxide (Al2O3), silicon oxide (SiO2) and / or zirconium oxide (ZrO2). Particularly suitable materials from which a support can be made include for example inorganic polymers, organic polymers, glasses, organic and inorganic crystals, minerals, oxides, ceramics, metals, especially precious metals, carbon and semiconductors. A particularly suitable organic polymer is a polymer based on polystyrene. Biopolymers, such as cellulose, dextran, agar, agarose and Sephadex, which may be functionalized, in particular as nitrocellulose or cyanogen bromide Sephadex, can be used as polymers which provide a solid support. In a third aspect of the invention, there is provided an apparatus for detecting the presence, absence or level of (i) a peptide comprising or consisting of SEQ ID No: 2 (T30), or a variant or fragment thereof, and / or (ii) a peptide comprising or consisting of SEQ ID No:3 (T14), or a variant or fragment thereof,in a sample, the apparatus comprising any one or more aptamers according to the first aspect, and optionally, a support. In certain embodiments, the invention provides reagents for use in an ELISA or ELISA-like assay, biosensor, a lateral flow test, or a functionalised electrode for detecting the presence, absence or level of T14 or T30 peptides in a sample. The apparatus according to the invention may be provided in a number of different formats. In certain embodiments, the invention provides apparatus for detecting the presence, absence or level of T14 or T30 peptides in a sample, the apparatus comprising an aptamer as described herein. In certain embodiments, the apparatus comprises a support as described herein. For example, in the absence of T14 or T30 peptides, the aptamer may be secured directly or indirectly to a support to immobilise it. In certain embodiments, the apparatus comprises a linker sequence as described herein. In certain embodiments, the aptamer of the invention is attached directly or indirectly (e.g. via a linker) to the support surface. For example, the aptamers may be immobilised through a linker which is chemically attached to the end of the aptamer to allow direct immobilisation of the aptamer. In certain embodiments, the linker sequence is a DNA or an RNA molecule or a mixed DNA / RNA molecule, wherein optionally the linker molecule comprises one or more modified nucleotides. In certain embodiments, the apparatus may be a biosensor. Therefore, in a fourth aspect of the invention, there is provided a biosensor, assay plate or test strip comprising any one or more aptamers according to the first aspect and, optionally, one or more detectable molecules. Biosensors are found in many different formats. In certain embodiments, the biosensor comprises the aptamer and a transducer which converts the binding event between the aptamer and T14 or T30 peptides into an electrically quantifiable signal. The biosensor may be comprised in a vessel or a probe or the like. In addition, the apparatus may further comprise other elements such as a signal processing device, output electronics, a display device, a data processing device, a data memory device and interfaces to other devices. In certain embodiments, a sample containing T14 or T30 peptides is brought into contact with the biosensor. T14 or T30 peptides may then be identified via the changes in the aptamer properties upon specific binding of T14 or T30 peptides to the aptamer. The sensitivity of the sensor may be influenced by the transducer used. The transducer converts the signal from the binding event, which is proportional to the concentration of the target molecule in the sample, into an electrically quantifiable measurement signal. Signalling occurs due to the molecular interaction between the aptamer and T14 or T30 peptides. With a biosensor according to the invention, qualitative, quantitative and / or semi-quantitative analytical information can be obtained. The measurement in optical transducers can be based on principles of photometry, whereby, for example, colour or luminescence intensity changes are detected. Optical methods include the measurement of fluorescence, phosphorescence, bioluminescence and chemiluminescence, infrared transitions and light scattering. The optical methods also include the measurement of layer thickness changes when T14 or T30 peptides is bound to the aptamer. The layer thickness can be measured, for example, by surface plasmon resonance (SPR), reflectometric interference spectroscopy (RIfS), biolayer interferometry (BLI) or similar. Furthermore, the interference on thin layers (SPR or RlfS) and the change of the evanescent field can be measured. Acoustic transducers use the frequency changes of a piezoelectric quartz crystal, which detects highly sensitive mass changes that occur when target binds to aptamer. The quartz crystal used is placed in an oscillating electric field and the resonant frequency of the crystal is measured. A mass change on the surface of the quartz crystal can be quantified. In certain embodiments, the apparatus is a BLI (Biolayer Interferometry) apparatus or similar apparatus. BLI is a label-free technology for measuring biomolecular interactions. It is an optical analytical technique that analyses changes in the interference pattern of white light reflected from two surfaces: a layer of immobilised ligand on the biosensor tip, and an internal reference layer. Any change in the number of molecules bound to the biosensor tip causes a shift in the interference pattern that can be measured in real-time. Only molecules binding to or dissociating from the biosensor can shift the interference pattern and generate a response profile on the BLI sensor. Unbound molecules, changes in the refractive index of the surrounding medium, or changes in flow rate do not affect the interference pattern. In certain embodiments, the apparatus may comprise a nanopore detecting platform (e.g. Resistive Pulse Sensing (RPS) or the like). Typically, such detection platforms allow the detection of any aptamer of the invention via the use of complementary DNA hairpins. For example, any aptamer moving through the pore may be affected by protein binding thus providing an indirect measure of protein binding. The invention also provides a test strip and / or lateral flow device comprising any aptamer or complex as described herein. Lateral flow devices may also be referred to as lateral flow tests, lateral flow assays and lateral flow immunoassays. Therefore, in a fifth aspect, there is provided a lateral flow device comprising one or more aptamers according to the first aspect, or the complex of the second aspect. In certain embodiments, the lateral flow device comprises a support onto which a linker sequence is attached. The linker sequence may be configured to hybridise to at least a portion of an aptamer as described herein. Any sample as described herein (e.g. a swab, blood, sputum or plasma sample) may be introduced. If the sample comprises T14 or T30 peptides, the aptamer may bind to the T14 or T30 peptides and undergo a conformational change, resulting in the aptamer disassociating from the linker sequence. Typically, however, the lateral flow device comprises a traditional LFD format in which the T14 or T30 peptides is ‘captured’ on a ‘test line’ compromising of an immobilised aptamer; followed by the detection with a second aptamer (which may be the same as the first aptamer) or antibody, which is conjugated to an appropriate detection molecule (e.g. latex bead, gold nanoparticles, fluorophore or similar). In certain embodiments, the apparatus may be suitable for use in assays such as ELISA (enzyme-linked immunosorbent assay) and variants of which are known to those skilled in the art. When aptamers are used in place of antibodies, the resulting assay is often referred to as an “ELONA” (enzyme-linked oligonucleotide assay), “ELASA” (enzyme linked aptamer sorbent assay), “ELAA” (enzyme-linked aptamer assay) or similar. Incorporating aptamers into these ELISA-like assay platforms can result in increased sensitivity, allow a greater number of analytes to be detected; including analytes for which there are no antibodies available and a wide range of outputs, since aptamers can be conjugated to multiple reporter molecules including fluorophores, quencher molecules and / or any other detection moiety as described herein. In certain embodiments, the apparatus may comprise a vessel. The aptamer of the invention may be immobilized via hybridization to a linker sequence in the vessel (e.g. the surface of the vessel). Alternatively, the aptamer of the invention may be directly immobilised on the surface of the vessel via a linker or functional group on the end of the aptamer. Thus, in a sixth aspect, there is provided functionalised electrode or biosensor surface comprising one or more aptamers according to the first aspect. In a seventh aspect, the invention provides use of any one or more aptamers as described herein, any complex as described herein, any biosensor or test strip as described herein or, any apparatus as described herein, including, for example, any ELISA or ELISA-like assay as described herein, any lateral flow test as described herein, any functionalised electrode or sensor surface as described herein, or the like, for detecting, enriching, separating and / or isolating: (i) a peptide comprising or consisting of SEQ ID No: 2 (T30), or a variant or fragment thereof, and / or (ii) a peptide comprising or consisting of SEQ ID No:3 (T14), or a variant or fragment thereof. In one embodiment, the peptide comprising or consisting of SEQ ID No: 2 (T30), or a variant or fragment thereof, and / or the peptide comprising or consisting of SEQ ID No:3 (T14), or a variant or fragment thereof may be detected, enriched, separated and / or isolated from a sample. Any appropriate sample may be used. In addition, samples may be obtained using any relevant approach or technique known in in the art. In one embodiment, the sample may be cerebrospinal fluid (CSF). In an eighth aspect, the invention provides a method of detecting the presence, absence or amount of (i) a peptide comprising or consisting of SEQ ID No: 2 (T30), or a variant or fragment thereof, and / or (ii) a peptide comprising or consisting of SEQ ID No:3 (T14), or a variant or fragment thereof, in a sample, the method comprising: (i) interacting the sample with any one or more aptamers as described herein; and (ii) detecting the presence, absence or amount of (i) a peptide comprising or consisting of SEQ ID No: 2 (T30), or a variant or fragment thereof, and / or (ii) a peptide comprising or consisting of SEQ ID No:3 (T14), or a variant or fragment thereof. Any appropriate sample may be used. In addition, samples may be obtained using any relevant approach or technique known in in the art. In one embodiment, the sample may be cerebrospinal fluid (CSF). In certain embodiments, the sample is biological. For example, the sample may comprise whole blood, leukocytes, peripheral blood mononuclear cells, plasma, serum, sputum, breath, urine, semen, saliva, meningeal fluid, amniotic fluid, glandular fluid, lymph fluid, nipple aspirate, bronchial aspirate, synovial fluid, joint aspirate, cells, a cellular extract, stool, tissue, a tissue biopsy or cerebrospinal fluid. In certain embodiments, the sample is a blood (e.g. plasma) sample. Alternatively, the sample may be a saliva or sputum (mucus or phlegm) sample. The sample may be pre-treated, such as by mixing, addition of enzymes, buffers, salt solutions or markers, or purified. In certain embodiments, the sample is an unobtrusive breath sample. For example, the breath sample may not require obtrusive collection as compared to a swab sample. Typically, the unobtrusive breath sample is obtained using a standard breathalyser. In certain embodiments, the sample is obtained by taking a swab test (e.g. throat and / or nose swab). For example, a sample may comprise at least two different regions from the same subject (e.g. back of throat and inside of nose). Alternatively, the sample may be a blood or urine or sweat sample. In the methods for detecting the presence, absence, or amount of T14 or T30 peptides in a sample, the sample may be interacted (i.e., contacted) with any aptamer as described herein. For example, the sample and aptamers as described herein may be incubated under conditions sufficient for at least a portion of the aptamer to bind to any T14 or T30 peptides in the sample. Any suitable conditions for binding between the aptamers as described herein and the T14 or T30 peptides may be used. In certain embodiments, the sample and aptamer are incubated at temperatures between about 20°C and about 37°C. In certain embodiments, the sample and aptamer may be diluted to different concentrations (e.g. at least about 1%, 5%, 10%, 20%, 25%, 30%, 40%, 50%, 60%, 70% 80% v / v or more) with appropriate buffers (e.g. PBS or other buffer composition known to those skilled in the art). In certain embodiments, the sample and aptamer may be incubated whilst shaking and / or mixing. In certain embodiments, the sample and aptamer are incubated for at least 1 minute, at least 5 minutes, at least 15 minutes, at least 1 hour or more. In certain embodiments, binding of the aptamer and T14 or T30 peptides leads to formation of an aptamer- T14 or T30 peptide complex. The binding or binding event may be detected, for example, visually, optically, photonically, electronically, acoustically, opto-acoustically, by mass, electrochemically, electro-optically, spectrometrically, enzymatically or otherwise chemically, biochemically or physically as described herein. The binding of aptamer and T14 or T30 peptide may be detected using any suitable technique. As discussed above, for example, binding of the aptamer and T14 or T30 peptide may be detected using a biosensor. In certain embodiments, binding of the aptamer and T14 or T30 peptide is detected using SPR, RlfS, BLI, LFD or ELONA as described herein, or other technique known to those skilled in the art. Advantageously, the aptamers of the invention allow detection of clinically pathological amounts of T14 or T30 peptides. The inventors have observed that the concentration of the T14 and / or T30 peptides varies between different biological samples. For example, in blood, the concentration of T14 / T30 in a healthy control subject may be about 100ng / ml, and double (i.e., around 200ng / ml) in a subject suffering from Alzheimer’s Disease. In CSF, the concentration of T14 / T30 in a healthy control subject may be about 60ng / ml, and double (i.e., around 120ng / ml) in a subject suffering from Alzheimer’s Disease. In nasal fluid, the concentration of T14 / T30 in a healthy control subject may be about 20-30ng / ml, and double (i.e., around 40-60ng / ml) in a subject suffering from Alzheimer’s Disease. Typically, the aptamers of the invention have a detection limit of less than about 10000pg / ml peptide, e.g. less than about 9000pg / ml, less than about 8000pg / ml, less than about 7000pg / ml, less than about 6000pg / ml, less than about 5000pg / ml, less than about 4000pg / ml, less than about 3000pg / ml, less than about 2000pg / ml, less than about 1000pg / ml, less than about 900pg / ml, less than about 800pg / ml, less than about 700pg / ml, less than about 600pg / ml, less than about 500pg / ml, less than about 400pg / ml, less than about 300pg / ml, less than about 200pg / ml, less than about 100pg / ml or less than about 50pg / ml T14 or T30 peptides. Typically, the aptamers of the invention have a detection range from about 50pg / ml to about 10000pg / ml T14 or T30 peptides. Thus, the aptamers are capable of binding to T14 or T30 peptides with high specificity and / or affinity and allow pathological ranges of active T14 or T30 peptides to be detected in a sample. Advantageously, the aptamers of the invention allow pathological ranges of T14 or T30 peptides to be detected in a sample in, for example, less than about 60 minutes, less than about 50 minutes. less than about 40 minutes, less than about 30 minutes, less than about 20 minutes, less than about 10 minutes, or less. In a ninth aspect, the invention provides a kit for detecting, quantifying and / or enriching (i) a peptide comprising or consisting of SEQ ID No: 2 (T30), or a variant or fragment thereof, and / or (ii) a peptide comprising or consisting of SEQ ID No:3 (T14), or a variant or fragment thereof, the kit comprising any one or more aptamers according to the first aspect. Typically, the kit also comprises a detectable molecule as described herein. In some embodiments, the kit further comprises instructions for use in accordance with any of the methods described herein. In certain embodiments, the kit further comprises a linker and / or support as described herein. Typically, the kit comprises further components for the reaction intended by the kit or the method to be carried out, for example components for an intended detection of enrichment, separation and / or isolation procedures. Examples are buffer solutions, substrates for a colour reaction, dyes or enzymatic substrates. In the kit, the aptamer may be provided in a variety of forms, for example pre-immobilised onto a support (e.g. solid support), freeze-dried or in a liquid medium. The kit of the invention may be used for carrying out any method described herein. It will be appreciated that the parts of the kit may be packaged individually in vials or in combination in containers or multi-container units. Typically, manufacture of the kit follows standard procedures which are known to the person skilled in the art. In certain embodiments, the kit may be used to capture and / or concentrate the virus as further described herein. For example, the invention may comprise a kit comprising an aptamer as described herein to help improve the sensitivity of any diagnostic tests for neurodegenerative disorders. It will be appreciated that features of the present disclosure are susceptible to being combined in various combinations without departing from the scope of the present disclosure as defined by the appended claims. In certain embodiments, the aptamers of the invention are prepared using principles of in vitro selection known in the art, that include iterative cycles of target binding, partitioning and preferential amplification of target binding sequences. In certain embodiments, the aptamers are selected from a nucleic acid molecule library such as a single-stranded DNA or RNA nucleic acid molecule library. Typically, the aptamers are selected from a library that is designed such that any selected aptamers need little to no adaptation to convert into any of the listed assay formats. In certain embodiments, the library comprises at least the following functional parts: a first primer binding region (P1), at least one randomised region (R) and a second primer binding region (P2). SEQ ID NO: 35 shows an exemplary nucleic acid sequence of first primer region (P1): 5' - CCA GTG TAG ACT ACT CAA TGC - 3' SEQ ID NO: 36 shows an exemplary nucleic acid sequence of second primer region (P2): 5' - GT ACT ATC CAC AGG TCA ACC -3’ Aptly, at least a portion of the randomised region (R) is involved in target molecule binding. The randomised region may be any suitable length. Typically, the randomised region is about 30 to 60 nucleic acid bases in length. For example, the randomised region may be about 40 nucleotides in length. Aptly, the primer regions may serve as primer binding sites for PCR amplification of the library and selected aptamers. Once selected, the aptamer may be further modified before being used e.g. to remove one or both primer sequences and / or parts of the randomised region not required for target binding. The skilled person would understand different primer sequences can be selected depending, for example, on the starting library and / or aptamer selection protocol. For example, the aptamers of the invention may comprise SEQ ID NO: 5-34. Thus, in certain embodiments the aptamers of the invention may be selected using the forward and reverse primer pair as set forth in SEQ ID NO: 35 and 36. In any of the aptamer sequences described herein, these primer sequences may be replaced with any alternative suitable primer sequence. The first primer region and / or second region may comprise a detectable label as described herein. For example, the first and / or second primer region may be fluorescently (e.g. FAM)-labelled. In certain embodiments, the first and / or second primer region primer are phosphate (PO4) labelled. In certain embodiments, the invention provides one or more aptamers that are capable of inhibiting the interaction between T14 and the nicotinic alpha-7 receptor (alpha7nAChR). Accordingly, in a tenth aspect, the invention provides any one or more aptamers according to the first aspect, for use as a medicament. In an eleventh aspect, the invention provides any one or more aptamers according to the first aspect, for use in the treatment, prevention or amelioration of a neurodegenerative disorder. In a twelfth aspect, there is provided a method of treating, preventing or ameliorating a neurodegenerative disorder in a subject, the method comprising administering, to a subject in need of such treatment, a therapeutically effective amount of one or more aptamers according to the first aspect. Preferably, the neurodegenerative disorder is selected from a group consisting of Alzheimer's disease; Parkinson's disease; Huntington's disease; Motor Neurone disease; Spinocerebellar type 1, type 2, and type 3; Amyotrophic Lateral Sclerosis (ALS); and Frontotemporal Dementia. Most preferably, the neurodegenerative disorder is Alzheimer’s disease. It will be appreciated that aptamers according to the invention may be used in a medicament which may be used in a monotherapy (i.e., use of the one or more aptamer of the first aspect), for treating, ameliorating, or preventing neurodegenerative disorder, such as Alzheimer’s disease. Alternatively, the aptamers according to the invention may be used as an adjunct to, or in combination with, known therapies for treating, ameliorating, or preventing Alzheimer’s disease, such as acetylcholinesterase inhibitors. The aptamers according to the invention may be combined in compositions having a number of different forms depending, in particular, on the manner in which the composition is to be used. Thus, for example, the composition may be in the form of a powder, tablet, capsule, liquid, ointment, cream, gel, hydrogel, aerosol, spray, micellar solution, transdermal patch, liposome suspension or any other suitable form that may be administered to a person or animal in need of treatment. It will be appreciated that the vehicle of medicaments according to the invention should be one which is well-tolerated by the subject to whom it is given, and preferably enables delivery of the peptide across the blood-brain barrier. It will be appreciated that the efficiency of any treatment for brain disorders depends on the ability of the candidate therapeutic aptamers to cross the blood- brain barrier (BBB). However, it is well-known that, during Alzheimer’s disease, the blood-brain barrier increases in permeability that could allow the aptamers of the invention to reach the central nervous system, indeed ideally only at the sites of degeneration where it is needed, i.e., where the BBB is compromised. Medicaments comprising aptamers according to the invention may be used in a number of ways. For instance, oral administration may be required, in which case the aptamers may be contained within a composition that may, for example, be ingested orally in the form of a tablet, capsule or liquid. An alternative option for administrating the aptamers would be to use a nasal spray, since aptamer administration by nasal spray reaches the brain faster and more efficiently than oral or intravenous ways of administration (see http: / / memoryzine.com / 2010 / 07 / 26 / nose-sprays-cross-blood-brain-barrier-faster- and-safer / ). Hence, compositions comprising aptamers of the invention may be administered by inhalation (e.g. intranasally). Compositions may also be formulated for topical use. For instance, creams or ointments may be applied to the skin, for example, adjacent the brain. Aptamers according to the invention may also be incorporated within a slow- or delayed-release device. Such devices may, for example, be inserted on or under the skin, and the medicament may be released over weeks or even months. The device may be located at least adjacent the treatment site, e.g. the head. Such devices may be particularly advantageous when long-term treatment with aptamers used according to the invention is required and which would normally require frequent administration (e.g. at least daily injection). In a preferred embodiment, medicaments according to the invention may be administered to a subject by injection into the blood stream or directly into a site requiring treatment. For example, the medicament may be injected at least adjacent the brain. Injections may be intravenous (bolus or infusion) or subcutaneous (bolus or infusion), or intradermal (bolus or infusion). It will be appreciated that the amount of the aptamer that is required is determined by its biological activity and bioavailability, which in turn depends on the mode of administration, the physiochemical properties of the aptamers and whether it is being used as a monotherapy or in a combined therapy. The frequency of administration will also be influenced by the half-life of the aptamers within the subject being treated. Optimal dosages to be administered may be determined by those skilled in the art, and will vary with the particular aptamers in use, the strength of the pharmaceutical composition, the mode of administration, and the advancement of the neurodegenerative disease. Additional factors depending on the particular subject being treated will result in a need to adjust dosages, including subject age, weight, gender, diet, and time of administration. Generally, a daily dose of between 0.001µg / kg of body weight and 10mg / kg of body weight of the aptamers according to the invention may be used for treating, ameliorating, or preventing neurodegenerative disease, depending upon which aptamer is used. More preferably, the daily dose is between 0.01μg / kg of body weight and 1mg / kg of body weight, and most preferably between approximately 0.1μg / kg and 10μg / kg body weight. The aptamers may be administered before, during or after onset of neurodegenerative disease. Daily doses may be given as a single administration (e.g. a single daily injection or inhalation of a nasal spray). Alternatively, the aptamer may require administration twice or more times during a day. As an example, aptamers may be administered as two (or more depending upon the severity of the neurodegenerative disease being treated) daily doses of between 0.07 μg and 700 mg (i.e., assuming a body weight of 70 kg). A patient receiving treatment may take a first dose upon waking and then a second dose in the evening (if on a two dose regime) or at 3- or 4-hourly intervals thereafter. Alternatively, a slow release device may be used to provide optimal doses of aptamers according to the invention to a patient without the need to administer repeated doses. Known procedures, such as those conventionally employed by the pharmaceutical industry (e.g. in vivo experimentation, clinical trials, etc.), may be used to form specific formulations of the aptamers according to the invention and precise therapeutic regimes (such as daily doses of the agents and the frequency of administration). The inventors believe that they are the first to suggest an anti- neurodegenerative disease composition, based on the use of an aptamer of the invention. Hence, in a thirteenth aspect of the invention, there is provided a pharmaceutical composition comprising a therapeutically effective amount of one or more aptamer according to the first aspect, and optionally a pharmaceutically acceptable vehicle. The pharmaceutical composition is preferably an anti-neurodegenerative disease composition, i.e., a pharmaceutical formulation used in the therapeutic amelioration, prevention or treatment of a neurodegenerative disorder in a subject, such as Alzheimer’s disease. The invention also provides in a fourteenth aspect, a process for making the pharmaceutical composition according to the thirteenth aspect, the process comprising combining a therapeutically effective amount of one or more aptamer according to the first aspect, with a pharmaceutically acceptable vehicle. The aptamer may preferably comprise: (a) a nucleic acid sequence selected from any one or more of SEQ ID NOs: 5- 34; (b) a nucleic acid sequence having at least about 85%, 90%, 95% or 99% sequence identity or more with any one or more of the sequences of (a); or (c) a nucleic acid sequence having at least about 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75 or more consecutive nucleotides of any one or more of the sequences of (a) or (b). A “subject” may be a vertebrate, mammal, or domestic animal. Hence, medicaments according to the invention may be used to treat any mammal, for example livestock (e.g. a horse), pets, or may be used in other veterinary applications. Most preferably, however, the subject is a human being. A “therapeutically effective amount” of peptide is any amount which, when administered to a subject, is the amount of active agent that is needed to treat the neurodegenerative disorder condition, or produce the desired effect. For example, the therapeutically effective amount of aptamer used may be from about 0.001 mg to about 800 mg, and preferably from about 0.01 mg to about 500 mg. It is preferred that the amount of aptamer is an amount from about 0.1 mg to about 100 mg. A “pharmaceutically acceptable vehicle” as referred to herein, is any known compound or combination of known compounds that are known to those skilled in the art to be useful in formulating pharmaceutical compositions. In one embodiment, the pharmaceutically acceptable vehicle may be a solid, and the composition may be in the form of a powder or tablet. A solid pharmaceutically acceptable vehicle may include one or more substances which may also act as flavouring agents, lubricants, solubilisers, suspending agents, dyes, fillers, glidants, compression aids, inert binders, sweeteners, preservatives, coatings, or tablet- disintegrating agents. The vehicle may also be an encapsulating material. In powders, the vehicle is a finely divided solid that is in admixture with the finely divided active agents according to the invention. In tablets, the aptamer may be mixed with a vehicle having the necessary compression properties in suitable proportions and compacted in the shape and size desired. The powders and tablets preferably contain up to 99% of the active agents. Suitable solid vehicles include, for example calcium phosphate, magnesium stearate, talc, sugars, lactose, dextrin, starch, gelatin, cellulose, polyvinylpyrrolidine, low melting waxes and ion exchange resins. In another embodiment, the pharmaceutical vehicle may be a gel and the composition may be in the form of a cream or the like. However, the pharmaceutical vehicle may be a liquid, and the pharmaceutical composition is in the form of a solution. Liquid vehicles are used in preparing solutions, suspensions, emulsions, syrups, elixirs and pressurized compositions. The aptamer according to the invention may be dissolved or suspended in a pharmaceutically acceptable liquid vehicle such as water, an organic solvent, a mixture of both or pharmaceutically acceptable oils or fats. The liquid vehicle can contain other suitable pharmaceutical additives such as solubilisers, emulsifiers, buffers, preservatives, sweeteners, flavouring agents, suspending agents, thickening agents, colours, viscosity regulators, stabilizers or osmo- regulators. Suitable examples of liquid vehicles for oral and parenteral administration include water (partially containing additives as above, e.g. cellulose derivatives, preferably sodium carboxymethyl cellulose solution), alcohols (including monohydric alcohols and polyhydric alcohols, e.g. glycols) and their derivatives, and oils (e.g. fractionated coconut oil and arachis oil). For parenteral administration, the vehicle can also be an oily ester such as ethyl oleate and isopropyl myristate. Sterile liquid vehicles are useful in sterile liquid form compositions for parenteral administration. The liquid vehicle for pressurized compositions can be a halogenated hydrocarbon or other pharmaceutically acceptable propellant. Liquid pharmaceutical compositions, which are sterile solutions or suspensions, can be utilized by, for example, intramuscular, intrathecal, epidural, intraperitoneal, intravenous and particularly subcutaneous injection. The aptamer may be prepared as a sterile solid composition that may be dissolved or suspended at the time of administration using sterile water, saline, or other appropriate sterile injectable medium. The aptamers and compositions of the invention may be administered orally in the form of a sterile solution or suspension containing other solutes or suspending agents (for example, enough saline or glucose to make the solution isotonic), bile salts, acacia, gelatin, sorbitan monoleate, polysorbate 80 (oleate esters of sorbitol and its anhydrides copolymerized with ethylene oxide) and the like. The aptamer used according to the invention can also be administered orally either in liquid or solid composition form. Compositions suitable for oral administration include solid forms, such as pills, capsules, granules, tablets, and powders, and liquid forms, such as solutions, syrups, elixirs, and suspensions. Forms useful for parenteral administration include sterile solutions, emulsions, and suspensions. It will be appreciated that the invention extends to any nucleic acid or peptide or variant, derivative or analogue thereof, which comprises substantially the amino acid or nucleic acid sequences of any of the sequences referred to herein, including variants or fragments thereof. The terms “substantially the amino acid / nucleotide / peptide sequence”, “variant” and “fragment”, can be a sequence that has at least 40% sequence identity with the amino acid / nucleotide / peptide sequences of any one of the sequences referred to herein, for example 40% identity with any of the sequences described herein. Amino acid / polynucleotide / polypeptide sequences with a sequence identity which is greater than 65%, more preferably greater than 70%, even more preferably greater than 75%, and still more preferably greater than 80% sequence identity to any of the sequences referred to are also envisaged. Preferably, the amino acid / polynucleotide / polypeptide sequence has at least 85% identity with any of the sequences referred to, more preferably at least 90% identity, even more preferably at least 92% identity, even more preferably at least 95% identity, even more preferably at least 97% identity, even more preferably at least 98% identity and, most preferably at least 99% identity with any of the sequences referred to herein. The skilled technician will appreciate how to calculate the percentage identity between two amino acid / polynucleotide / polypeptide sequences. In order to calculate the percentage identity between two amino acid / polynucleotide / polypeptide sequences, an alignment of the two sequences must first be prepared, followed by calculation of the sequence identity value. The percentage identity for two sequences may take different values depending on:- (i) the method used to align the sequences, for example, ClustalW, BLAST, FASTA, Smith-Waterman (implemented in different programs), or structural alignment from 3D comparison; and (ii) the parameters used by the alignment method, for example, local vs global alignment, the pair-score matrix used (e.g. BLOSUM62, PAM250, Gonnet etc.), and gap-penalty, e.g. functional form and constants. Having made the alignment, there are many different ways of calculating percentage identity between the two sequences. For example, one may divide the number of identities by: (i) the length of shortest sequence; (ii) the length of alignment; (iii) the mean length of sequence; (iv) the number of non-gap positions; or (v) the number of equivalenced positions excluding overhangs. Furthermore, it will be appreciated that percentage identity is also strongly length dependent. Therefore, the shorter a pair of sequences is, the higher the sequence identity one may expect to occur by chance. Hence, it will be appreciated that the accurate alignment of protein or DNA sequences is a complex process. The popular multiple alignment program ClustalW (Thompson et al., 1994, Nucleic Acids Research, 22, 4673-4680; Thompson et al., 1997, Nucleic Acids Research, 24, 4876-4882) is a preferred way for generating multiple alignments of proteins or DNA in accordance with the invention. Suitable parameters for ClustalW may be as follows: For DNA alignments: Gap Open Penalty = 15.0, Gap Extension Penalty = 6.66, and Matrix = Identity. For protein alignments: Gap Open Penalty = 10.0, Gap Extension Penalty = 0.2, and Matrix = Gonnet. For DNA and Protein alignments: ENDGAP = -1, and GAPDIST = 4. Those skilled in the art will be aware that it may be necessary to vary these and other parameters for optimal sequence alignment. Preferably, calculation of percentage identities between two amino acid / polynucleotide / polypeptide sequences may then be calculated from such an alignment as (N / T)*100, where N is the number of positions at which the sequences share an identical residue, and T is the total number of positions compared including gaps and either including or excluding overhangs. Preferably, overhangs are included in the calculation. Hence, a most preferred method for calculating percentage identity between two sequences comprises (i) preparing a sequence alignment using the ClustalW program using a suitable set of parameters, for example, as set out above; and (ii) inserting the values of N and T into the following formula:- Sequence Identity = (N / T)*100. Alternative methods for identifying similar sequences will be known to those skilled in the art. For example, a substantially similar nucleotide sequence will be encoded by a sequence which hybridizes to DNA sequences or their complements under stringent conditions. By stringent conditions, the inventors mean the nucleotide hybridises to filter-bound DNA or RNA in 3x sodium chloride / sodium citrate (SSC) at approximately 45ºC followed by at least one wash in 0.2x SSC / 0.1% SDS at approximately 20-65ºC. Alternatively, a substantially similar polypeptide may differ by at least 1, 2, 3, 4, but less than 5, 10, 20, 50 or 100 amino acids from the sequences described herein. Due to the degeneracy of the genetic code, it is clear that any nucleic acid sequence described herein could be varied or changed without substantially affecting the sequence of the protein encoded thereby, to provide a functional variant thereof. Suitable nucleotide variants are those having a sequence altered by the substitution of different codons that encode the same amino acid within the sequence, thus producing a silent (synonymous) change. Other suitable variants are those having homologous nucleotide sequences but comprising all, or portions of, sequence, which are altered by the substitution of different codons that encode an amino acid with a side chain of similar biophysical properties to the amino acid it substitutes, to produce a conservative change. For example small non-polar, hydrophobic amino acids include glycine, alanine, leucine, isoleucine, valine, proline, and methionine. Large non-polar, hydrophobic amino acids include phenylalanine, tryptophan and tyrosine. The polar neutral amino acids include serine, threonine, cysteine, asparagine and glutamine. The positively charged (basic) amino acids include lysine, arginine and histidine. The negatively charged (acidic) amino acids include aspartic acid and glutamic acid. It will therefore be appreciated which amino acids may be replaced with an amino acid having similar biophysical properties, and the skilled technician will know the nucleotide sequences encoding these amino acids. Further features of certain embodiments of the present invention are described below. The practice of embodiments of the present invention will employ, unless otherwise indicated, conventional techniques of molecular biology, microbiology, recombinant DNA technology and immunology, which are within the skill of those working in the art. Most general molecular biology, microbiology recombinant DNA technology and immunological techniques can be found in Sambrook et al, Molecular Cloning, A Laboratory Manual (2001) Cold Harbor-Laboratory Press, Cold Spring Harbor, N.Y. or Ausubel et al., Current protocols in molecular biology (1990) John Wiley and Sons, N.Y. Unless defined otherwise, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this disclosure belongs. For example, the Concise Dictionary of Biomedicine and Molecular Biology, Juo, Pei-Show, 2nd ed., 2002, CRC Press; The Dictionary of Cell and Molecular Biology, 3rd ed., Academic Press; and the Oxford University Press, provide a person skilled in the art with a general dictionary of many of the terms used in this disclosure. Units, prefixes and symbols are denoted in their Système International de Unitese (SI) accepted form. Numeric ranges are inclusive of the numbers defining the range. Unless otherwise indicated, amino acid sequences are written left to right in amino to carboxy orientation and nucleic acid sequences are written left to right in 5′ to 3′ orientation. All of the features described herein (including any accompanying claims, abstract and drawings), and / or all of the steps of any method or process so disclosed, may be combined with any of the above aspects in any combination, except combinations where at least some of such features and / or steps are mutually exclusive. For a better understanding of the invention, and to show how embodiments of the same may be carried into effect, reference will now be made, by way of example, to the accompanying Figures, in which:- Figure 1 shows preliminary screening data to determine which of the target(s); T14, T15 or T30 (upper, middle, lower respectively) are suitable for aptamer selection, and which buffer (1, 2 or 3) promotes a concentration dependent interaction with target loaded beads (white bars) above the non-specific interaction with the blank beads (black bars). Figure 2 shows Selection Stringency Maps used in the generation of aptamers against the T14 (upper) and T30 (lower) peptides. This table includes details of the amount of aptamer library used, amount of target peptide used, the amount of counter selection target, the incubation times, the number of washes etc. Figure 3 shows Biolayer Interferometry data for the aptamer populations isolated against the T14 peptide. The raw data (left plot) shows target loading on the sensor probe (660-960 sec), an established baseline (1560-1680 sec), and then association (1680-1800 sec) and dissociation (1800-1920 sec) of example aptamer populations. Background corrected data (right plot) shows only the association and dissociation phases. The unrefined naïve library is used as a reference sample, and shows a low interaction with the immobilised T14 peptide. Exemplar refined aptamer population T148R show increased binding to the immobilised T14 peptide, indicating a higher proportion of target binding sequences. Figure 4 shows Biolayer Interferometry data for the aptamer populations isolated against the T30 peptide. The raw data (left plot) shows target loading on the sensor probe (660-960 sec), an established baseline (1560-1680 sec), and then association (1680-1800 sec) and dissociation (1800-1920 sec) of example aptamer populations. Background corrected data (right plot) shows only the association and dissociation phases. The unrefined naïve library is used as a reference sample, and shows a low interaction with the immobilised T30 peptide. Exemplar refined aptamer populations T307R & T309R show increased binding to the immobilised T30 peptide, indicating a higher proportion of target binding sequences. Examples The inventors have observed that T14 and T30 biomarker peptides are surprisingly present in very small, but detectable, concentrations in saliva, nasal discharge and pin-prick blood. The inventors have isolated a series of aptamers which specifically bind to the T14 or T30 peptides. Such sample types may be commonly analysed using a lateral flow test (LFT), which, unlike CSF and venous / arterial blood, are painless, socially acceptable by the general public, low cost, can be used frequently, and provide very fast and accurate results. In the example experiments, standard reagents and buffers free from contamination are used. EXAMPLE 1 – Aptamer selection Aptamer selection target peptide preparation Synthetic peptides encompassing targets T14, T15 and T30 (SEQ ID NO: 3, 4 and 2, respectively) were supplied by NeuroBio. The peptides were synthesised by Genosphere Biotechnologies (France). The peptides were characterised by UV spectroscopy for quality control purposes. The peptides were immobilised onto separate batches of NHS activated magnetic beads (Bioclone Inc., USA; Product code FI-114), according to manufacturer’s protocols. The peptide loading density was determined spectrophotometrically. Aptamer library and oligonucleotides The aptamer selection process was carried out, starting from a synthetic ssDNA oligonucleotide sequences of an aptamer library (manufactured by IDT, Belgium). The nucleotide sequences of the aptamer library have the following structure (in a 5’ to 3’ direction): P1 – R – P2, wherein P1 is a first primer region, R is a randomized region (40 nucleotides in length in this case) and P2 is a further primer region wherein R or a portion thereof are involved in target molecule binding. The following modified primers were used in the amplification of the oligomers by means of PCR: fluorescein (FAM)-labelled forward primer (P1) with the sequence: 5' - 5FAM / CCA GTG TAG ACT ACT CAA TGC - 3' (SEQ ID NO: 35) and PO4-modified reverse primer (P2) with the sequence: 5' / 5Phos / GGT TGA CCT GTG GAT AGT AC-3' (SEQ ID NO: 37). Establishing parameters for aptamer selection A preliminary study was carried out to determine which of the target peptides T14, T15 or T30 (SEQ ID NO: 3, 4 and 2, respectively) are most amenable to aptamer selection, to identify the most appropriate selection buffer and required target excess for the selection process. The naïve aptamer library was diluted into each of three aptamer selection buffers and aliquoted across a 96 well plate, such that each well contains 1.65 picomoles of buffered aptamer library. A concentration gradient of the T14, T15 or T30 immobilised Magnetic beads was prepared and aliquoted across separate 96 well plates, to give a seven-point target gradient consisting of different ‘fold-excess’ of target (and a row of ‘target-negative’ controls). An equivalent gradient of target-negative beads (blank magnetic beads with nothing immobilised) was also prepared. The binding assay was carried out on Biomek NX liquid handling robots (Beckman Coulter). In this binding assay, the buffered aptamer library is added to the bead gradient, these are mixed and incubated for one hour at room temperature, to allow aptamers to bind to the immobilised target or blank beads. After incubation, the beads are separated on a 96 well magnetic plate rack, and unbound aptamers are removed. The beads are washed with the respective buffer, to remove any weak binding aptamers. The bound aptamers are recovered from the beads by resuspending the beads in PCR mix and thermal- cycled (according to standard manufacturer protocols). This results in the elution and amplification of the bound aptamers. The amount of aptamers recovered from each target concentration is then quantified by qPCR. ‘Recovery data’ (as shown in Figure 1) is compared to determine the amount of aptamer bound to the target immobilised and blank beads, in each of the selection buffers. The ‘optimum’ selection buffer is chosen based on the ratio of aptamer biding to target loaded vs blank beads. The amount of target to be used in selection is also chosen from this assay, based on the amount of aptamer recovered. For the aptamer selection against both T14 and T30 peptides, the best performing buffer is 50mM MES pH6.2, 5mM MgCl2, 1mM CaCl2, 77.5mM NaCl, 4.5mM KCl, 20mM Na2SO4, 0.01% (v / v) Tween-20, 0.01% (w / v) BSA. For the T14 target peptide, a 53-fold excess of target was chosen for the first round of selection. For the T30 target peptide, a 13-fold excess of target was chosen for the first round of selection. In vitro selection of an aptamer population against the T14 and T30 peptides The selection process consisted of iterative selection rounds with increasingly stringent selection conditions (as defined in Figure 2). In Cycle 1, 166pmol of naïve aptamer library is incubated with the target immobilised beads, using the binding conditions established in the preliminary binding study. The beads are washed to remove loosely bound aptamers, then remaining aptamers are eluted in PCR mix and amplified as carried out in the preliminary binding study. The recovered amplified aptamer library is purified using AxyPrep Mag PCR Clean-up Kit (Axygen Biosciences, USA), digested with Lambda exonuclease (EURx, Poland) at 37 °C according to manufacturer’s protocol. The nascent ssDNA is purified using AxyPrep Mag PCR Clean-up kit to produce a purified and enriched single stranded DNA library for the subsequent aptamer selection cycle. In Cycle 2 (and all subsequent rounds), the same process is followed but aptamer-target incubations are carried out with increasingly stringent conditions. The details of this ‘stringency map’ (target ratios, incubation times, washes etc) are defined in Figure 1. As the aptamer selection progresses the target excess and positive incubation time decreases, and the negative excess and negative incubation time increases. The number of washes also increases, to increase selection stringency. EXAMPLE 2 – Characterisation of the aptamer populations After aptamer selection, the refined aptamer populations were assessed for the ability to bind to the respective target peptides using a Biolayer interferometry assay. The experiments described here were conducted using an Octet RED384 instrument (Sartorius) based on manufacturer’s defined protocols. The target peptides were immobilised onto the surface of AR2G BLI biosensor probes (Octet® Amine Reactive Second Generation (AR2G) Dip & Read Biosensors, Sartorius) following manufacturer protocols. The aptamer populations were prepared at 50nM in 1x aptamer selection buffer (50mM MES pH6.2, 5mM MgCl2, 1mM CaCl2, 77.5mM NaCl, 4.5mM KCl, 20mM Na2SO4, 0.01% (v / v) Tween-20, 0.01% (w / v) BSA). All buffer / blank / baseline interactions were carried out in 1x aptamer selection buffer. The interaction between the immobilised T14 peptide and each of the isolated aptamer populations was monitored (as shown in Figure 3). All data was reference corrected using a blank sensor probe (no immobilised aptamer) to allow correction of buffer effects. Aptamer populations isolated against the T30 peptide were also characterised using the same assay format, with T30 peptide immobilised onto the biosensor probes (as shown in Figure 4). EXAMPLE 3 – Identification of individual aptamers Next Generation Sequencing and data Pools which have improved target relative to the naïve library, are analysed by Next Generation Sequencing (NGS) to identify potential candidate monoclonal aptamer sequences. The population analysis is carried out using an Ion PGM Ion Torrent Next Generation Sequencing system. Libraries were prepared according to manufacturer protocols (Ion Torrent™ Ion Plus Fragment Library kit, ThermoFisher), and barcoded following manufacturer protocols (Ion Xpress™ Barcode Adapters 1-96 Kit). Barcoded populations were then templated onto Ion Sphere Particles (ISP) following manufacturer protocols (Ion OneTouch™ 2 System). After successful templating the prepared templated ISPs were processed and loaded onto an Ion 318™ Chip Kit v2 BC following manufacturer protocols and the samples run using the Ion PGM Ion Torrent Next Generation Sequencing system. Sequence reads were then analysed in Linux to identify enriched candidate sequences within each population. In house python scripts were used to process the sequencing data and trim each sequence so that only the variable region is present in the data. Datasets were then clustered using FastAptameR2.0 (https: / / fastaptamer2.missouri.edu / ) to group similar sequences into families or ‘clusters’. The highest read sequence from each cluster is then taken forward as the candidate sequence for synthesis and subsequent pairwise screening by Biolayer Interferometry (BLI) on the Octet RED384 instrument (Sartorius). This process allows screening structurally distinct aptamer sequences which should bind to different regions on the T14 or T30 peptides. Identification of individual aptamers Individual aptamer candidate sequences were synthesised using standard solid phase phosphoramidite oligonucleotide synthesis methods. DNA phosphoramidites (Thermo Fisher Scientific) were used to prepare the candidate Optimers using a Dr Oligo 768 High throughput oligonucleotide synthesiser (Biolytic Inc), following manufacturer’s instructions. Synthesised oligonucleotides were deprotected using AMA (1:1 v / v solution of 28% ammonium hydroxide and 40% methylamine) and then purified using Glen-Pak DNA purification cartridges following the manufacturer’s instructions. Optimers were analysed by polyacrylamide gel electrophoresis before being used in screening assays. Each individual aptamer was then analysed for binding to their respective target (T14 or T30 peptides); using the BLI assay described above. EXAMPLE 4 – Identification of aptamer pairs Identification of aptamer pairs To identify aptamer pairs which bind to distinct epitopes on the T14 or T30 peptides target, a sandwich assay was the conducted using the Octet RED384 instrument (Sartorius). In this assay the best performing aptamer was immobilised onto streptavidin coated biosensor probes and then interacted with either the T14 or T30 peptides. Secondary aptamers were then screened for additional binding to distinct epitopes. An additional positive response is indicative of a likely aptamer-pair. All other conditions used in this assay are as described in Example 2. For any observed response from this secondary aptamer, a control assay was carried out in which the aptamers were associated with buffer (no T14 or T30 peptide present in solution) and associated with the secondary aptamer pair to identify aptamer-aptamer interactions causing the observed signal. Determination of aptamer binding affinity to the T14 or T30 peptides The affinity of chosen aptamers is determined using the BLI assay according to the protocol described above. The target peptides are immobilised onto the surface of AR2G BLI biosensor probes (as described above) and then interaction monitored with a concentration series of each aptamer diluted in 1x aptamer selection buffer). KD values were calculated using the Octet data analysis software (Octet Data Analysis 8.0,), using a 1:1 binding model. EXAMPLE 5 – Identification of minimal functional aptamer fragment Identification of minimal functional aptamer fragment A minimal functional aptamer fragment (Optimer®) was identified for several of the isolated and characterised aptamers. Briefly, a panel of fragments representing different regions of the full-length aptamer, were produced by solid phase synthesis. Each of these individual fragments was screened for interaction with immobilised target peptide, using the BLI assay (according to the protocol described above). The BLI screen shows which fragments retain their binding affinity and which fragments have lost their binding function. These binding and non-binding fragments are mapped onto the full-length aptamer sequence to identify the minimal functional fragment (Optimer™). EXAMPLE 6 – Aptamers and Optimers bind to T14 or T30 peptides in buffered nasal swab samples In order to use in simple point- care it is desirable that the aptamers and Optimers are capable of recognising and binding to their target in a readily accessible sample matrix, with minimal processing. To demonstrate this proof-of-concept, the aptamers and respective Optimers, were immobilised onto BLI sensor probes and assessed for the ability to bind to the S1 subunit of the SARS-CoV-2 spike protein when spiked into buffered nasal swab samples. Briefly, nasal swab samples were obtained from healthy volunteers, buffered with 1x aptamer selection buffer, then combined in equal volumes. The buffered nasal sample was spiked with the T14 or T30 peptide. Spiked samples were incubated with the immobilised aptamers or Optimers and interactions monitored using the BLI binding assay described above. BLI data shows a clear interaction between the immobilised aptamers and Optimers, and the T14 or T30 peptide in buffered nasal samples. This demonstrates the potential of these aptamers and Optimers to recognise and bind the peptide in patient nasal samples; without the need for expensive or laborious sample processing steps. EXAMPLE 7 – Optimers isolated against the T14 or T30 peptides, bind their targets in a simple Lateral Flow Test format Lateral Flow Tests are simple test formats that can be run without the need for special laboratory equipment. They are a preferred assay format for simple, rapid mass screening of large numbers of samples. In this test format, one of the binding pair of Optimers is immobilised on the ‘test line’, the other Optimer is immobilised onto the surface of a Gold Nanoparticle and deposited in the ‘conjugate pad’. When the test is run, a sample is applied to the ‘sample pad’. The material runs along the lateral flow membrane by capillary action. If the target peptide is present in the sample, it is captured on the immobilised Optimer in the ‘test line’. Optimer coated Gold Nanoparticles are also captured on the ‘test line’ to give a visible signal. In the absence of the target peptide, the Optimer coated Gold Nanoparticles are not captured on the ‘test line’, giving a ‘blank’ test line. A ‘control line’ is used to show that the test has run correctly. In this case the ‘control line’ consists of an immobilised ‘capture oligonucleotide’ that is complimentary to the Optimer on the Gold Nanoparticles. Hybridization between the immobilised ‘capture oligonucleotide’ and the Optimer on the Gold Nanoparticles leads to the formation of a ‘control line’. The aptamers described herein have been isolated using synthetic peptides (SEQ ID NO: 2 to 4). Preparation of the Gold Nanoparticles In this example the preferred Optimers isolated against T14 and T30 peptide, were prepared with a 5’ thiol group to allow the Optimer to be immobilised onto 40nm OD5 Gold Nanoparticles (BBI Solutions, UK). Briefly, 1ml of OD5 gold colloid was transferred into a 1.5ml Eppendorf tube and centrifuged for 10 minutes @ 4000 x g to pellet the Gold Nanoparticles. The supernatant was removed, and the pellet resuspend in 500µl of 0.22µm filtered deionised water to create an OD10 nanoparticle stock.0.5mg of aptamer was applied directly to 1ml of the gold colloid solution and incubated for 1 minute at room temperature.25µl of 0.5M Tri-Sodium Citrate was added to the gold / aptamer solution, mixed gently by pipetting, and incubated for a further 10 minutes at room temperature.17.5µl of 2M Sodium chloride was added to the aptamer / gold solution and mixed gently by pipetting, then incubated for a further 20 minutes at room temperature on a plate shaker to agitate the mix.50µl of 2M Sodium Chloride was added to the aptamer / gold solution and mixed again by gentle pipetting, then incubated for a further 40 minutes at room temperature on a plate shaker to agitate the mix. The aptamer conjugated gold colloid was then centrifuged at 4000 x g for 15 minutes to form a pellet. The supernatant was carefully removed and discarded, and the pellet was resuspended with 500µl of 1x PBS with 0.05% Tween20. The aptamer / gold mixture was centrifuged again at 4000 x g for 15 minutes to re-form the pellet. The supernatant was removed, and the pellet resuspended in 500µl of 1x Phosphate Buffered Saline supplemented with 1mM Magnesium Chloride. The aptamer / gold mixture was pelleted a final time at 4000 x g for 15 minutes and the pellet was resuspended in 333µl 1x Phosphate buffered Saline, 5% sucrose, 3% BSA, 1% Tween20 (Gold drying buffer) Final gold OD = 15. Preparation of the derivatised nitrocellulose membrane Preparation of both test and control line aptamers follow the same initial procedure. The preferred Optimer and ‘capture oligonucleotide’ were each synthesised with a 5’ biotin group. A separate mix was prepared for each oligonucleotide, containing 33.4µM of the respective oligonucleotide and 1mg / ml polystreptavidin e.g. for a 200µl final volume of ‘test line’ or ‘control line’ stock; 55.6µl of 120µM biotinylated oligonucleotide stock was combined with 87.3µl 1x Phosphate Buffered Saline and 57.1µl of 3.5mg / ml polystreptavidin stock. The combined mixture was incubated at room temperature for 1 hour. The isoflow dispenser was set up using the following parameters: ‘test line’ dispense nozzle to 7mm and ‘control line’ dispense nozzle to 13mm. Both lines were dispensed at half rate (0.5µl / mm) across a 30cm length band. The sprayed NC was marked to denote the start and end of plotted lines and any potential inconstant plotting along the length of the band. The membrane was then dried by passing through a drying tunnel (hedinair) at 10mm / sec @ 60°C. All membranes were stored within a heat-sealed foil pouch containing desiccant until required for assembly. Strip lamination The gold conjugate pad (17mm width) was prepared with aptamer colloid 1.1. Prepared NC membrane 1.2.22mm grade 222 sink pad 1.3.12mm 8951 conjugate pad (sample pad) 1.4.60mm single side adhesive backing card 1.5. Kinematic cutter The tape cover was removed from backing card and the laminator height was set to allow a 20mm gap from the bottom of the backing card to the bottom of the NC. The NC was placed with the ‘test line’ in the lower most position. The ‘sink pad’ was positio ne d against the top edge of the backing card such that a 7mm overlap with the NC was created (see diagram below). The ‘Conjugate pad’ was placed 5mm from the bottom of the backing card, to create a 2mm overlap with the NC (see diagram below). The ‘Sample pad’ was then aligned with the bottom of the backing card, to create a 7mm overlap with 'Conjugate pad’ (see diagram below). The band was then laminated and cut into individual 5mm strips and assembled into standard single sample well housing. A tion i t m w p r r o concentrations (and a negative control sample with no peptide material) in extraction buffer (mentioned above) from a master stock.80µl of each sample in the dilution series was pipetted onto a separate device. The test was then left to run for 10 minutes. Any readings after this time are classified as a e a control line has formed within the running time. Running the test assay – clinical samples Prior to sample collection, the donor was asked to gently blow their nose, then gently swab the anterior nasal cavity with the sterile swab (~5 rotations per nostril). The swab was immediately placed in the extraction tube containing 400µl extraction buffer (1M NaCl, 300mM Tris, 0.1% Tween20, 0.2% BSA, 0.05% pH 8.5) and rotated back and forth 10 times. The swab was gently squeezed when withdrawing from the extraction tube to maximise the sample recovery. The cap was closed on the extraction tube before inverting it for ~5 seconds to allow sample to pool into the filter in the dropper nozzle. The bottle was then gently squeezed to slowly add 3 drops of sample into the sample well of the Lateral Flow Device. Care was taken to ensure that the sample was taken into the device in the first 10 seconds of application. If it did not run, a fourth drop was added. The test was then left to run for 10 minutes. Any readings after this time are classified as invalid and ensure a control line has formed within the running time. The reader’s attention is directed to all papers and documents which are filed concurrently with or previous to this specification in connection with this application and which are open to public inspection with this specification, and the contents of all such papers and documents are incorporated herein by reference. 5

Claims

Claims 1. One or more aptamers capable of binding to: (i) a peptide comprising or consisting of SEQ ID No: 2 (T30), or a variant or fragment thereof, and / or (ii) a peptide comprising or consisting of SEQ ID No:3 (T14), or a variant or fragment thereof.

2. One or more aptamers according to claim 1, wherein the one or more aptamers bind to T15 (SEQ ID No:4).

3. One or more aptamers according to either claim 1 or claim 2, wherein the one or more aptamers bind to T14 (SEQ ID No: 3) and one or more aptamers bind to the T15 region (SEQ ID No: 4) of T30 (SEQ ID No: 2).

4. One or more aptamers according to any preceding claim, wherein the one or more aptamers specifically bind to a T14 region of the T30 peptide and / or the T15 region of the T30 peptide and / or a non-competing region of the T14 region of the T30 peptide.

5. One or more aptamers according to any preceding claim, wherein the aptamers are DNA aptamers, optionally wherein the aptamers are at least 15 nucleotides long and less than 120 nucleotides long.

6. One or more aptamers according to any preceding claim, wherein the one or more aptamers comprise: (a) a nucleic acid sequence selected from any one or more of SEQ ID NOs: 5- 34; (b) a nucleic acid sequence having at least about 85%, 90%, 95% or 99% sequence identity or more with any one or more of the sequences of (a); or (c) a nucleic acid sequence having at least about 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75 or more consecutive nucleotides of any one or more of the sequences of (a) or (b).

7. One or more aptamers according to any preceding claim, wherein the one or more aptamers are capable of binding to the T14 region of the peptide and comprise: (a) a nucleic acid sequence selected from any one or more of SEQ ID NOs: 5- 17;(b) a nucleic acid sequence having at least about 85%, 90%, 95% or 99% sequence identity or more with any one or more of the sequences of (a); or (c) a nucleic acid sequence having at least about 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75 or more consecutive nucleotides of any one or more of the sequences of (a) or (b).

8. One or more aptamers according to any preceding claim, wherein the one or more aptamers are capable of binding to the T30 region of the peptide and comprise: (a) a nucleic acid sequence selected from any one or more of SEQ ID NOs: 18- 34; (b) a nucleic acid sequence having at least about 85%, 90%, 95% or 99% sequence identity or more with any one or more of the sequences of (a); or (c) a nucleic acid sequence having at least about 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75 or more consecutive nucleotides of any one or more of the sequences of (a) or (b).

9. One or more aptamers according to any preceding claim, wherein two or more aptamers bind to two or more different regions of the T14 or T30 peptides.

10. One or more aptamers according to any preceding claim, wherein a first aptamer is capable of binding to the T14 or T30 peptides and a second aptamer is capable of binding to either a different region of the T14 or T30 peptides or to the T15 region of the T30 peptide.

11. One or more aptamers according to either claim 9 or claim 10, wherein at least a pair of aptamers comprises: (a) a first aptamer comprising a nucleic sequence selected from any one of SEQ ID NOs 5-34, or a sequence having at least about 85%, 90%, 95% or 99% sequence identity or more with any one of SEQ ID NOs 5-34; and (b) a second aptamer comprising a nucleic sequence selected from any one of SEQ ID NOs 5-34, or a sequence having at least about 85%, 90%, 95% or 99% sequence identity or more with any one of SEQ ID NOs 5-34.

12. One or more aptamers according to any preceding claim, wherein two or more aptamers are selected from any two or more nucleic acids selected from: - SEQ ID NOs 5-17 (or variants thereof); and / or- SEQ ID NOs 18-34 (or variants thereof).

13. A complex comprising one or more aptamers according to any one of claims 1-12, and a detectable molecule.

14. Apparatus for detecting the presence, absence or level of (i) a peptide comprising or consisting of SEQ ID No: 2 (T30), or a variant or fragment thereof, and / or (ii) a peptide comprising or consisting of SEQ ID No:3 (T14), or a variant or fragment thereof, in a sample, the apparatus comprising any one or more aptamers according any one of claims 1-12, and optionally, a support.

15. A biosensor, assay plate or test strip comprising any one or more aptamers according any one of claims 1-12 and, optionally, one or more detectable molecules.

16. A lateral flow device comprising one or more aptamers according any one of claims 1-12, or the complex according to claim 13.

17. A functionalised electrode or biosensor surface comprising one or more aptamers according any one of claims 1-12.

18. Use of any one or more aptamers according any one of claims 1-12, the complex according to claim 13, the apparatus according to claim 14, the biosensor, assay plate or test strip according to claim 15, the lateral flow device according to claim 16, the functionalised electrode or biosensor surface according to claim 17, including, for example, any ELISA or ELISA-like assay, for detecting, enriching, separating and / or isolating: (i) a peptide comprising or consisting of SEQ ID No: 2 (T30), or a variant or fragment thereof, and / or (ii) a peptide comprising or consisting of SEQ ID No:3 (T14), or a variant or fragment thereof.

19. A method of detecting the presence, absence or amount of: (i) a peptide comprising or consisting of SEQ ID No: 2 (T30), or a variant or fragment thereof, and / or (ii) a peptide comprising or consisting of SEQ ID No:3 (T14), or a variant or fragment thereof, in a sample, the method comprising: (i) interacting the sample with any one or more aptamers according any one of claims 1-12; and(ii) detecting the presence, absence or amount of (i) a peptide comprising or consisting of SEQ ID No: 2 (T30), or a variant or fragment thereof, and / or (ii) a peptide comprising or consisting of SEQ ID No:3 (T14), or a variant or fragment thereof.

20. A kit for detecting, quantifying and / or enriching (i) a peptide comprising or consisting of SEQ ID No: 2 (T30), or a variant or fragment thereof, and / or (ii) a peptide comprising or consisting of SEQ ID No:3 (T14), or a variant or fragment thereof, the kit comprising any one or more aptamers according any one of claims 1-12.

21. One or more aptamers according any one of claims 1-12, for use as a medicament.

22. One or more aptamers according any one of claims 1-12, for use in the treatment, prevention or amelioration of a neurodegenerative disorder.

23. One or more aptamers, for use according to claim 22, wherein the neurodegenerative disorder is selected from a group consisting of Alzheimer's disease; Parkinson's disease; Huntington's disease; Motor Neurone disease; Spinocerebellar type 1, type 2, and type 3; Amyotrophic Lateral Sclerosis (ALS); and Frontotemporal Dementia.

24. One or more aptamers, for use according to either claim 22 or claim 23, wherein the neurodegenerative disorder is Alzheimer’s disease.

25. A pharmaceutical composition comprising a therapeutically effective amount of one or more aptamer according any one of claims 1-12, and optionally a pharmaceutically acceptable vehicle.

26. A process for making the pharmaceutical composition according to claim 25, the process comprising combining a therapeutically effective amount of one or more aptamer according any one of claims 1-12, with a pharmaceutically acceptable vehicle.

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