Cell-penetrating peptide sequences

Abstract

This invention discloses cell-penetrating cyclic peptides. These peptides can be used to deliver peptides and other biologically active components into cells. Formulations containing cell-penetrating cyclic peptides are also described.

Description

Cell-penetrating peptide sequences Cross-reference to related applications This application claims priority to U.S. Application No. 62 / 425,550, filed November 22, 2016; U.S. Application No. 62 / 425,438, filed November 22, 2016; U.S. Application No. 62 / 438,141, filed December 22, 2016; and U.S. Application No. 62 / 507,483, filed May 17, 2017, the entire contents of each of which are incorporated herein by reference for all purposes. Federal sponsorship research statement This invention was made with government support under National Institutes of Health grants GM062820 and GM110208. The U.S. government has certain rights in this invention. This invention relates to cell-penetrating peptide sequences. Cell membranes pose significant challenges for drug discovery, especially for biologic agents such as peptides, proteins, and nucleic acids. One potential strategy to overcome the membrane barrier and deliver biologic agents into cells is to attach them to "cell-penetrating peptides (CPPs)". Despite three decades of research, the fundamental basis of CPP activity remains unclear. CPPs that enter cells via endocytosis must leave the endocytic vesicles to reach the cytosol. Unfortunately, the endosomal membrane has proven to be a significant barrier to cytoplasmic delivery of these CPPs. Thus, what is needed are novel cell-penetrating peptides and compositions comprising such peptides that can be used to deliver agents to a variety of cell types. The compositions and methods disclosed herein address these and other needs. In some embodiments, the disclosure provides a cyclic peptide according to one of Formulas I-A to I-E: , , , , or where AA 1 , AA 2 , AA 3 , AA 4 , AA 5 , AA 6 , AA 7 , AA 8 , AA 9, and AA 10 each of which, when present, is independently selected from amino acids; and wherein: AA 1 , AA 2 , AA 3 , AA 4 , AA 5 , AA 6 , AA 7 , AA 8 , AA 9 , or AA 10 two or three of which, when present, are arginine, and the remaining amino acids are amino acids other than arginine; and AA 1 , AA 2 , AA 3 , AA 4 , AA 5 , AA 6 , AA 7 , AA 8 , AA 9 , or AA 10 at least two of which, when present, are independently hydrophobic amino acids. In some embodiments, each hydrophobic amino acid is independently selected from the group consisting of phenylglycine, leucine, isoleucine, norleucine, methionine, phenylalanine, homophenylalanine, cyclohexylalanine, tyrosine, piperidine-2-carboxylate, tryptophan, proline, 3-(3-benzothienyl)-alanine, and naphthylalanine, each of which is optionally substituted with one or more substituents. In other embodiments, each hydrophobic amino acid is independently piperidine-2-carboxylate, naphthylalanine, tryptophan, 3-(3-benzothienyl)-alanine, or phenylalanine, each of which is optionally substituted with one or more substituents. In some embodiments, at least one hydrophobic amino acid has a hydrophobicity greater than or equal to that of phenylalanine. In certain embodiments, at least two of the amino acids have relative chirality. In further embodiments, at least two of the amino acids have the same chirality. In some embodiments, an arginine is adjacent to a hydrophobic amino acid. In further embodiments, the arginine has the same chirality as the adjacent hydrophobic amino acid. In some embodiments, at least two arginines are adjacent to each other. In other embodiments, three arginines are adjacent to each other. In some embodiments, at least two hydrophobic amino acids are adjacent to each other. In other embodiments, at least three hydrophobic amino acids are adjacent to each other. In some embodiments, any four adjacent amino acids are AA H2 -AA H1 -R-r, AA H2 -AA H1 -r-R, R-r-AA H1 -AA H2 、or r-R-AA H1 -AA H2 ,where AA H1 and AA H2 each independently is a hydrophobic amino acid. Thus, in various embodiments, the cyclic peptides disclosed herein (e.g., cyclic peptides according to Formula I, and I-A to I-E) have a structure according to any one of Formulas II-A to II-D: 、 、and where: AA H1 and AA H2 each independently is a hydrophobic amino acid; AAu and AAz are each independently any amino acid each time they appear; and at most one of each AAu and each AAz is arginine; and where: each of m and n independently is a number from 0 to 6, provided that at least one of m or n is not 0 and the total number of amino acids is from 6 to 10. In some embodiments, AA H1 and AA H2Each of which is independently piperidine-2-carboxylate, naphthylalanine, tryptophan, 3-(3-benzothienyl)-alanine, or phenylalanine, each of which is optionally substituted with one or more substituents. In other embodiments, AA H1 and AA H2 Each of which is independently a hydrophobic amino acid having a hydrophobicity greater than or equal to that of phenylalanine (e.g., using any scale provided in Table 2 herein). In still other embodiments, AA H1 is naphthylalanine. In yet still other embodiments, AA H1 and AA H2 are naphthylalanine. In some embodiments, AA H1 is a hydrophobic amino acid having a large solvent-accessible surface area (SASA) in the side chain. In further embodiments, the large SASA is at least about 200 Å 2 . In still further embodiments, the large SASA is in the range of about 200 Å 2 to about 1,000 Å 2 . In other embodiments, AA H2 is a hydrophobic amino acid having a SASA of the side chain less than or equal to the SASA of the side chain of AA H1 . In still other embodiments, when any AA U or any AA Z is a hydrophobic amino acid, the hydrophobic amino acid has a side chain with a SASA less than that of AA H1 . In some embodiments, AA H1 and AA H2 have the same or opposite chirality. In some other embodiments, AA H1 and AA H2 have opposite chirality. In still other embodiments, AA H1 has the same chirality as the adjacent arginine. In certain embodiments, the peptides disclosed herein include one of the following sequences: AA H2 -AA H1 -R-r-R, AA H2 -AA H1 -R-r-r, AA H2 -AA H1 -r-R-R, AA H2 -AA H1 -r-R-r, R-R-r-AA H1 -AA H2 , r-R-r-AA H1 -AA H2 , r-r-R-AA H1 -AA H2 , or R-r-R-AA H1 -AA H2 . In other embodiments, the peptides have one of the following sequences: AA H2 -LAA H1 -R-r-R, AA H2 -DAA H1 -r-R-r, r-R-r-DAA H1 -AA H2 , or R-r-R-LAA H1 -AA H2 . In some embodiments, the relative cytosolic delivery efficiency of the cyclic peptides disclosed herein is improved by an amount in the range of about 50% to about 500% compared to cyclo(FФRRRRQ) (SEQ ID NO:10). In some embodiments, the cyclic peptide has a relative cytosolic delivery efficiency that is improved by about 175% to about 250% compared to cyclo(FФRRRRQ) (SEQ ID NO:10). In some such embodiments, the cyclic peptide comprises the following sequence: FfFRr, such as cyclo(FfFRrQ) (SEQ ID NO:96). In other embodiments, the cyclic peptide has a relative cytosolic delivery efficiency that is improved by about 150% to about 400% compared to cyclo(FФRRRRQ) (SEQ ID NO:10). In some such embodiments, the cyclic peptide comprises the following sequence: fFfrRr (SEQ ID NO:132), such as cyclo(fFfrRrQ) (SEQ ID NO:97). In still other embodiments, the cyclic peptide has a cytosolic delivery efficiency that is improved by about 75% to about 275% compared to cyclo(FФRRRRQ) (SEQ ID NO:10). In some such embodiments, the cyclic peptide comprises the following sequence: fFfRrR (SEQ ID NO:133), such as cyclo(fFfRrRQ) (SEQ ID NO:98). In yet still other embodiments, the cyclic peptide has a cytosolic delivery efficiency that is improved by about 150% to about 250% compared to cyclo(FФRRRRQ) (SEQ ID NO:10). In some such embodiments, the cyclic peptide comprises the following sequence: FfFrRr (SEQ ID NO:134), such as cyclo(FfFrRrQ) (SEQ ID NO:99). In some embodiments, the cyclic peptide has a cytosolic delivery efficiency that is improved by about 200% to about 450% compared to cyclo(FФRRRRQ) (SEQ ID NO:10). In some such embodiments, the cyclic peptide comprises the following sequence: fFɸrRr (SEQ ID NO:135), such as cyclo(fFɸrRrQ) (SEQ ID NO:100). In other embodiments, the peptide has a cytosolic delivery efficiency that is improved by about 250% to about 450% compared to cyclo(FФRRRRQ) (SEQ ID NO:10). In some such embodiments, the cyclic peptide comprises the following sequence: fФfrRr (SEQ ID NO:136), such as cyclo(fФfrRrQ) (SEQ ID NO:101). Also disclosed herein are cyclic peptides according to Formulas III-A through III-D: , , , or wherein: AA 1, AA 2 , AA 3 , and AA 4 Each of those in is independently selected from amino acids; AA U and AA Z Each of those in, each time it appears, is independently selected from amino acids; Each of m and n is a number from 0 to 6, provided that at least one of m or n is not 0; X n is its cargo portion; L is the linker portion; wherein: AA 1 , AA 2 , AA 3 , AA 4 , each AA U , and each AA Z Two or three of those in are arginine, and the remaining amino acids are amino acids other than arginine; AA 1 , AA 2 , AA 3 , AA 4 , each AA U , and each AA Z At least two of those in are independently hydrophobic amino acids; and wherein when X n is attached to AA U , m is not 0. In some embodiments, each hydrophobic amino acid is independently selected from the group consisting of phenylglycine, leucine, isoleucine, norleucine, methionine, phenylalanine, homophenylalanine, cyclohexylalanine, tyrosine, piperidine-2-carboxylate, tryptophan, proline, 3-(3-benzothienyl)-alanine, and naphthylalanine, each of which is optionally substituted with one or more substituents. In other embodiments, each hydrophobic amino acid is independently piperidine-2-carboxylate, naphthylalanine, tryptophan, 3-(3-benzothienyl)-alanine, or phenylalanine, each of which is optionally substituted with one or more substituents. In some embodiments, at least one hydrophobic amino acid has a hydrophobicity greater than or equal to that of phenylalanine. In certain embodiments, at least two of the amino acids have relative chirality. In further embodiments, at least two of the amino acids have the same chirality. In some embodiments, one arginine is adjacent to a hydrophobic amino acid. In further embodiments, the arginine has the same chirality as the adjacent hydrophobic amino acid. In some embodiments, at least two arginines are adjacent to each other. In other embodiments, three arginines are adjacent to each other. In some embodiments, at least two hydrophobic amino acids are adjacent to each other. In other embodiments, at least three hydrophobic amino acids are adjacent to each other. In some embodiments, any four adjacent amino acids are AA H2 -AA H1 -R-r, AA H2 -AA H1 -r-R, R-r-AA H1 -AA H2 、or r-R-AA H1 -AA H2 where AA H1 and AA H2 each of which is independently a hydrophobic amino acid. In some embodiments, the cyclic peptides of Formulas III-A to III-D have a structure according to any one of Formulas IV-A to IV-P: 、 、 、 、 、 , , , , , , , , , , , wherein AA H1 and AA H2 each independently is a hydrophobic amino acid. In some embodiments, AA H1 and AA H2 each independently is piperidine-2-carboxylate, naphthylalanine, tryptophan, 3-(3-benzothienyl)-alanine, or phenylalanine, each of which is optionally substituted with one or more substituents. In other embodiments, AA H1 and AA H2 each independently is a hydrophobic amino acid having a hydrophobicity greater than or equal to that of phenylalanine (e.g., using any scale provided in Table 2 herein). In still other embodiments, AA H1 is naphthylalanine. In yet still other embodiments, AA H1 and AA H2 are naphthylalanine. In some embodiments, AA H1 is a hydrophobic amino acid having a large solvent-accessible surface area (SASA) in the side chain. In further embodiments, the large SASA is at least about 200 Å 2 . In still further embodiments, the large SASA is in the range of about 200 Å 2 to about 1,000 Å 2 . In other embodiments, AA H2 is a hydrophobic amino acid having a SASA of the side chain less than or equal to the SASA of the side chain of AA H1 . In still other embodiments, when any AA U or any AA Z When the hydrophobic amino acid is, the hydrophobic amino acid has a side chain with a SASA less than AA H1 of the SASA. In some embodiments, AA H1 and AA H2 have the same or opposite chirality. In some other embodiments, AA H1 and AA H2 have opposite chirality. In still other embodiments, AA H1 has the same chirality as the adjacent arginine. In certain embodiments, the peptides disclosed herein include one of the following sequences: AA H2 -AA H1 -R-r-R, AA H2 -AA H1 -R-r-r, AA H2 -AA H1 -r-R-R, AA H2 -AA H1 -r-R-r, R-R-r-AA H1 -AA H2 、r-R-r-AA H1 -AA H2 、r-r-R-AA H1 -AA H2 、or R-r-R-AA H1 -AA H2 。In other embodiments, the peptides have one of the following sequences: AA H2 -LAA H1-R-r-R, AA H2 -DAA H1 -r-R-r, r-R-r-DAA H1 -AA H2 、 or R-r-R-LAA H1 -AA H2 。 Peptides containing V-A to V-D are also disclosed herein: , , , or , where: AA H1 and AA H2 each of which is independently selected from hydrophobic amino acids; AA U and AA Z is independently selected from amino acids each time it appears, and each AA U and each AA Z at most one of which is arginine; and each of m and n is a number from 0 to 6, provided that at least one of m or n is not 0. In some embodiments, the amino group at the N-terminus or the carboxylic acid ester group at the C-terminus of any one of the formulas V-A to V-D independently forms a peptide bond. In other embodiments, the peptides of formulas V-A to V-D further comprise a cyclizing moiety for forming a cyclic peptide. In still other embodiments, the cyclizing moiety independently forms a peptide bond with the amino group at the N-terminus or the carboxylic acid ester group at the C-terminus of any one of the formulas V-A to V-D. In some embodiments, the peptides of formulas V-A to V-D further comprise a cargo moiety X n where at least one atom or bond is replaced by a bond connecting to X n of. In some embodiments, AA H1 and AA H2 each independently is piperidine-2-carboxylate, naphthylalanine, tryptophan, 3-(3-benzothienyl)-alanine, or phenylalanine, each of which is optionally substituted with one or more substituents. In some embodiments, AA H1 and AA H2 Each of which is independently a hydrophobic amino acid having a hydrophobicity greater than or equal to that of phenylalanine. In some embodiments, AA H1 is naphthylalanine. In some embodiments, AA H1 and AA H2 is naphthylalanine. In some embodiments, AA H1 is a hydrophobic amino acid having a large solvent-accessible surface area (SASA) in the side chain. In further embodiments, the large SASA is at least about 200 Å 2 . In still further embodiments, the large SASA is in the range of about 200 Å 2 to about 1,000 Å 2 . In other embodiments, AA H2 is a hydrophobic amino acid having a SASA of the side chain less than or equal to the SASA of the side chain of AA H1 . In still other embodiments, when any AA U or any AA Z is a hydrophobic amino acid, the hydrophobic amino acid has a side chain with a SASA less than that of AA H1 . In some embodiments, AA H1 and AA H2 have the same or opposite chirality. In some other embodiments, AA H1 and AA H2 have opposite chirality. In still other embodiments, AA H1 has the same chirality as the adjacent arginine. In certain embodiments, the peptides of Formulas V-A to V-D comprise one of the following sequences: AA H2 -AA H1 -R-r-R, AA H2 -AA H1 -R-r-r, AA H2 -AA H1 -r-R-R, AA H2 -AA H1 -r-R-r, R-R-r-AA H1 -AA H2 , r-R-r-AA H1 -AA H2 , r-r-R-AA H1 -AA H2 , or R-r-R-AA H1 -AA H2 . In other embodiments, the peptides have one of the following sequences: AA H2 -LAA H1 -R-r-R, AA H2 -DAA H1 -r-R-r, r-R-r-DAA H1 -AA H2 , or R-r-R-LAA H1 -AA H2 . In some embodiments, a peptide comprising any one of Formulas V-A to V-D has a cytosolic delivery efficiency in an amount that is improved by about 50% to about 500% compared to Cyclo(FФRRRRQ) (SEQ ID NO:10). In some embodiments, the peptides comprise the following sequences: FfFRrR (SEQ ID NO:131). In other embodiments, the peptides comprise the following sequences: fFfrRr (SEQ ID NO:132). In still other embodiments, the peptides comprise the following sequences: fFfRrR (SEQ ID NO:133). In yet still other embodiments, the peptides comprise the following sequences: FfFrRr (SEQ ID NO:134). In even still other embodiments, the peptides comprise the following sequences: fFɸrRr (SEQ ID NO:135). In some embodiments, the peptides comprising any one of Formulas V-A to V-D comprise the following sequence: fФfrRr (SEQ ID NO:136). In various embodiments, the present disclosure provides methods of treating or diagnosing a patient in need thereof, comprising administering a cyclic peptide disclosed herein. In various embodiments, the present disclosure provides compositions comprising a cyclic peptide described herein. Definitions Throughout the description and claims of this specification, the term "comprise" and other forms of the term such as "comprising" and "comprises" mean including but not limited to, and are not intended to exclude, for example, other additives, components, integers, or steps. As used in the description and the appended claims, the singular forms "a", "an", and "the" include plural referents unless the context clearly dictates otherwise. Thus, for example, reference to "a composition" includes mixtures of two or more such compositions, reference to "an agent" includes mixtures of two or more such agents, reference to "the component" includes mixtures of two or more such components, and the like. "Optional" or "optionally" means that the event or circumstance described thereafter may or may not occur, and the description includes examples where the event or circumstance occurs and examples where it does not occur. Ranges may be expressed herein as from “about” a particular value and / or to “about” another particular value. When such a range is expressed, another aspect includes from a particular value and / or to another particular value. Similarly, when values are expressed as approximations by use of the antecedent “about,” it will be understood that the particular value forms another aspect. It will be further understood that the endpoints of each of the ranges are significant with respect to the other endpoint and independent of the other endpoint. It will also be understood that when a range is provided, that range encompasses every value and sub-range within that range. As used herein, “subject” refers to an individual. Thus, “subject” can include domestic animals (such as cats, dogs, etc.), livestock (such as cows, horses, pigs, sheep, goats, etc.), laboratory animals (such as mice, rabbits, rats, guinea pigs, etc.), and birds. “Subject” can also include mammals such as primates or humans. Thus, a subject can be a human or a veterinary patient. The term “patient” refers to a subject under the treatment of a clinician such as a physician. The term “inhibit” refers to reducing an activity, a reaction, a condition, a disease, or other biological parameter. This can include, but is not limited to, completely ablating an activity, a reaction, a condition, or a disease. This can also include, for example, a 10% reduction in an activity, a reaction, a condition, or a disease as compared to a native or control level. Thus, the reduction can be a 10, 20, 30, 40, 50, 60, 70, 80, 90, 100%, or any amount in between reduction as compared to a native or control level. “Reduce” or other forms of the term such as “reducing” or “reduction” mean decreasing an event or a characteristic (such as tumor growth). It should be understood that this generally relates to some standard or expected value, in other words is relative, but does not necessarily require reference to a standard or relative value. For example, “reduces tumor growth” means decreasing the growth rate of a tumor relative to a standard or a control. "Prevent" or other forms of the term such as "preventing" or "prevention" mean to stop a particular event or characteristic, to stabilize or delay the development or progression of a particular event or characteristic, or to minimize the chance that a particular event or characteristic will occur. Prevention does not require a comparison to a control, as it is generally more absolute than, for example, reduction. As used herein, it is possible to reduce but not prevent something, but that which is reduced may also be prevented. Similarly, it is possible to prevent but not reduce something, but that which is prevented may also be reduced. It should be understood that the use of reduction or prevention, unless specifically indicated otherwise, also explicitly discloses the use of the other term. For example, the term "prevent" or "suppress" may refer to a treatment that prevents or slows the onset of a disease or condition or reduces the severity of a disease or condition in advance. Thus, if a treatment can treat a disease in a subject having symptoms of the disease, it may also prevent or suppress the disease in a subject in which some or all of the symptoms have not yet appeared. The term "treatment" refers to the medical management of a patient with the intention of curing, improving, stabilizing, or preventing a disease, pathologic condition, or disorder. This term includes active treatment, i.e., treatment specifically directed toward the improvement of a disease, pathologic condition, or disorder, and also causal treatment, i.e., treatment directed toward the removal of the cause of the relevant disease, pathologic condition, or disorder. In addition, this term includes palliative treatment, i.e., treatment designed to relieve symptoms rather than cure a disease, pathologic condition, or disorder; prophylactic treatment, i.e., treatment aimed at minimizing or partially or completely suppressing the development of the relevant disease, pathologic condition, or disorder; and supportive treatment, i.e., treatment adopted to supplement another specific therapy aimed at improving the relevant disease, pathologic condition, or disorder. The term "anticancer" refers to the ability to treat or control cell proliferation and / or tumor growth at any concentration. The term "therapeutically effective" means that the amount of the composition used is sufficient to improve one or more causes or symptoms of a disease or disorder. The improvement only needs to be a reduction or change and does not necessarily need to be an elimination. The term "pharmaceutically acceptable" refers to those compounds, materials, compositions, and / or dosage forms that are within the scope of reasonable medical judgment suitable for contact with human and animal tissues without excessive toxicity, irritation, allergic response, or other problems or complications and that meet a reasonable benefit / risk ratio. The term "carrier" means a compound, composition, substance, or structure that, when combined with a compound or composition, aids or facilitates the preparation, storage, administration, delivery, effectiveness, selectivity, or any other characteristic of the compound or composition for its intended use or purpose. For example, a carrier can be selected to minimize any degradation of the active ingredient and any adverse reactions in the subject. As used herein, the term "pharmaceutically acceptable carrier" refers to sterile aqueous or non-aqueous solutions, dispersions, suspensions, or emulsions, and sterile powders that are used to reconstitute sterile injectable solutions or dispersions immediately prior to use. Examples of suitable aqueous and non-aqueous carriers, diluents, solvents, or vehicles include water, ethanol, polyols (such as glycerol, propylene glycol, polyethylene glycol, and the like), carboxymethyl cellulose and its suitable mixtures, vegetable oils (such as olive oil), and injectable organic esters such as ethyl oleate. Appropriate fluidity can be maintained, for example, by the use of coating materials such as lecithin, by maintaining the required particle size in the case of a dispersion, and by the use of surfactants. These compositions may also contain adjuvants such as preservatives, wetting agents, emulsifying agents, and dispersing agents. Prevention of microbial action can be ensured by including various antibacterial and antifungal agents such as parabens, chlorobutanol, phenol, sorbic acid, and the like. It may also be desirable to include isotonic agents such as sugars, sodium chloride, and the like. Prolonged absorption of injectable pharmaceutical forms can be achieved by including agents that delay absorption such as aluminum monostearate and gelatin. Injectable depot forms are prepared by forming a microcapsule matrix of the drug in biodegradable polymers such as polylactic acid-polyglycolide, poly(orthoesters), and poly(anhydrides). The rate of drug release can be controlled according to the ratio of the drug to the polymer and the nature of the specific polymer employed. Depot injectable formulations can also be prepared by encapsulating the drug in liposomes or microemulsions that are compatible with body tissues. Injectable formulations can be sterilized, for example, by filtration through a bacteria-retaining filter, or by incorporating a sterilizing agent in the form of a sterile solid composition that can be dissolved or dispersed in sterile water or other sterile injectable medium immediately prior to use. Suitable inert carriers can include sugars such as lactose. Desirably, at least 95% by weight of the active ingredient particles have an effective particle size in the range of 0.01 to 10 microns. The terms "peptide", "protein", and "polypeptide" are used interchangeably and refer to natural or synthetic molecules that contain two or more amino acids that are linked by the carboxyl group of one amino acid to the α-amino group of another amino acid. As used herein, the term "adjacent" refers to two contiguous amino acids that are linked by a covalent bond. As used herein, the term "chirality" refers to the "D" and "L" isomers of amino acids. The term "acyl" refers to the group -C(O)R, where R is hydrogen, alkyl, alkenyl, alkynyl, aryl, heteroaryl, cycloalkyl, or heterocyclic group as defined herein. Unless otherwise specifically stated in the specification, the acyl group may be optionally substituted. "Alkyl (Alkyl or alkyl group)" refers to a fully saturated, straight-chain or branched hydrocarbon chain radical having one to twelve carbon atoms, and which is attached to the remainder of the molecule by a single bond. Alkyl groups containing any number of carbon atoms from 1 to 12 are included. An alkyl group containing up to 12 carbon atoms is C 1 -C 12 alkyl, an alkyl group containing up to 10 carbon atoms is C 1 -C 10 alkyl, an alkyl group containing up to 6 carbon atoms is C 1 -C 6 alkyl and an alkyl group containing up to 5 carbon atoms is C 1 -C 5 alkyl. C 1 -C 5 alkyl includes C 5 alkyl, C 4 alkyl, C 3 alkyl, C 2 alkyl and C 1 alkyl (i.e., methyl). C 1 -C 6 alkyl includes C 1 -C 5 all of the above portions of alkyl but also includes C 6 alkyl. C 1 -C 10 An alkyl group includes C 1 -C 5 alkyl groups and C 1 -C 6 all of the above portions of the alkyl group, but also includes C 7 , C 8 , C 9 and C 10 alkyl groups. Similarly, C 1 -C 12 alkyl groups includes all of the foregoing portions, but also includes C 11 and C 12 alkyl groups. C 1 -C 12 Non-limiting examples of alkyl groups include methyl, ethyl, n-propyl, isopropyl, sec-propyl, n-butyl, isobutyl, sec-butyl, tert-butyl, n-pentyl, tert-pentyl, n-hexyl, n-heptyl, n-octyl, n-nonyl, n-decyl, n-undecyl, and n-dodecyl. Unless otherwise specifically stated in the specification, the alkyl group may be optionally substituted. "Alkenyl (Alkenyl or alkenyl group)" refers to a straight-chain or branched hydrocarbon chain radical having two to twelve carbon atoms and having one or more carbon-carbon double bonds. Each alkenyl group is attached to the other part of the molecule by a single bond. Alkenyl groups containing any number of carbon atoms from 2 to 12 are included. Alkenyl groups containing up to 12 carbon atoms are C 2 -C 12 alkenyl groups, alkenyl groups containing up to 10 carbon atoms are C 2 -C 10 alkenyl groups, alkenyl groups containing up to 6 carbon atoms are C 2 -C 6 alkenyl groups and alkenyl groups containing up to 5 carbon atoms are C 2 -C 5 Alkenyl. C 2 -C 5 Alkenyl includes C 5 Alkenyl, C 4 Alkenyl, C 3 Alkenyl, and C 2 Alkenyl. C 2 -C 6 Alkenyl includes C 2 -C 5 All of the above alkenyl groups but also include C 6 Alkenyl. C 2 -C 10 Alkenyl includes C 2 -C 5 Alkenyl and C 2 -C 6 All of the above alkenyl moieties, but also include C 7 , C 8 , C 9 and C 10 Similarly, C 2 -C 12 Alkenyl includes all of the aforementioned moieties, but also includes C 11 and C 12 Alkenyl. C 2 -C 12Non-limiting examples of alkenyl include ethenyl (vinyl), 1-propenyl, 2-propenyl (allyl), isopropenyl, 2-methyl-1-propenyl, 1-butenyl, 2-butenyl, 3-butenyl, 1-pentenyl, 2-pentenyl, 3-pentenyl, 4-pentenyl, 1-hexenyl, 2-hexenyl, 3-hexenyl, 4-hexenyl, 5-hexenyl, 1-heptenyl, 2-heptenyl, 3-heptenyl, 4-heptenyl, 5-heptenyl, 6-heptenyl, 1-octenyl, 2-octenyl, 3-octenyl, 4-octenyl, 5-octenyl, 6-octenyl, 7-octenyl, 1-nonenyl, 2-nonenyl, 3-nonenyl, 4-nonenyl, 5-nonenyl, 6-nonenyl, 7-nonenyl, 8-nonenyl, 1-decenyl, 2-decenyl, 3-decenyl, 4-decenyl, 5-decenyl, 6-decenyl, 7-decenyl, 8-decenyl, 9-decenyl, 1-undecenyl, 2-undecenyl, 3-undecenyl, 4-undecenyl, 5-undecenyl, 6-undecenyl, 7-undecenyl, 8-undecenyl, 9-undecenyl, 10-undecenyl, 1-dodecenyl, 2-dodecenyl, 3-dodecenyl, 4-dodecenyl, 5-dodecenyl, 6-dodecenyl, 7-dodecenyl, 8-dodecenyl, 9-dodecenyl, 10-dodecenyl, and 11-dodecenyl. Unless otherwise specifically stated in the specification, the alkyl group may be optionally substituted. "Alkoxy" refers to the group -OR, where R is an alkyl, alkenyl, alkynyl, cycloalkyl, or heterocyclic group as defined herein. Unless otherwise specifically stated in the specification, the alkoxy group may be optionally substituted. "Alkylcarbamoyl" refers to the group -O-C(O)-NR a R b where R a and R b are the same or different and independently are an alkyl, alkenyl, alkynyl, aryl, heteroaryl, cycloalkyl, or heterocyclic group as defined herein, or R a R b may combine together to form a heterocyclic group as defined herein. Unless otherwise specifically stated in the specification, the alkylcarbamoyl group may be optionally substituted. "Alkylcarboxamidyl" refers to the group –C(O)-NR aR b , wherein R a and R b are the same or different and are independently an alkyl, alkenyl, alkynyl, aryl, heteroaryl, cycloalkyl, cycloalkenyl, cycloalkynyl, or heterocyclic group as defined herein, or R a R b may combine together to form a cycloalkyl as defined herein. Unless otherwise specifically stated in the specification, the alkylcarboxamide group may be optionally substituted. "Alkoxycarbonyl" means the group -C(O)OR, wherein R is an alkyl, alkenyl, alkynyl, aryl, heteroaryl, cycloalkyl, cycloalkenyl, cycloalkynyl, or heterocyclic group as defined herein. Unless otherwise specifically stated in the specification, the alkoxycarbonyl may be optionally substituted. "Alkylthio" means -SR or -S(O) n=1-2 -R, wherein R is an alkyl, alkenyl, alkynyl, cycloalkyl, cycloalkenyl, cycloalkynyl, or heterocyclic group as defined herein. Unless otherwise specifically stated in the specification, the alkylthio may be optionally substituted. "Arylthio" means -SR or -S(O) n=1-2 -R, wherein R is an aryl or heteroaryl as defined herein. Unless otherwise specifically stated in the specification, the arylthio may be optionally substituted. "Alkynyl (or alkynyl group)" means a straight-chain or branched hydrocarbon chain radical having two to twelve carbon atoms and having one or more carbon-carbon triple bonds. Each alkynyl group is attached to the rest of the molecule by a single bond. Alkynyl groups containing any number of carbon atoms from 2 to 12 are included. Alkynyl groups containing up to 12 carbon atoms are C 2 -C 12 alkynyl, alkynyl groups containing up to 10 carbon atoms are C 2 -C 10 alkynyl, alkynyl groups containing up to 6 carbon atoms are C 2 -C 6 alkynyl and alkynyl groups containing up to 5 carbon atoms are C 2 -C 5 Alkynyl. C 2 -C 5 Alkynyl groups include C 5 Alkynyl, C 4 Alkynyl, C 3 Alkynyl, and C 2 Alkynyl. C 2 -C 6 Alkynyl groups include C 2 -C 5 All of the above parts of alkynyl but also include C 6 Alkynyl. C 2 -C 10 Alkynyl groups include C 2 -C 5 Alkynyl and C 2 -C 6 All of the above parts of alkynyl, but also include C 7 , C 8 , C 9 and C 10 Similarly, C 2 -C 12 Alkynyl includes all of the aforementioned moieties, but also includes C 11 and C 12 Alkynyl. C 2 -C 12 Non-limiting examples of alkenyl include ethynyl, propynyl, butynyl, pentynyl, and the like. Unless specifically stated otherwise in the specification, an alkyl group may be optionally substituted. "Aryl" refers to a hydrocarbon ring system radical containing hydrogen, 6 to 18 carbon atoms, and at least one aromatic ring. For the purposes of the present invention, the aryl radical can be a monocyclic, bicyclic, tricyclic, or tetracyclic ring system, which can include fused or bridged ring systems. Aryl radicals include, but are not limited to, those derived from vinylanthracene, vinylnaphthalene, vinylphenanthrene, anthracene, azulene, benzene, , acenaphthylene, fluorene, as-indacene, s-indacene, indane, indene, naphthalene, acenaphthylene, phenanthrene, , pyrene, and terphenyl aryl radicals. Unless otherwise specifically stated in the specification, the term "aryl" is intended to include optionally substituted aryl radicals. "Aryloxy" refers to the group -OAr, where Ar is an aryl or heteroaryl as defined herein. Unless otherwise specifically stated in the specification, the aryloxy can be optionally substituted. "Cycloalkyl" refers to a stable non-aromatic monocyclic or polycyclic fully saturated hydrocarbon radical composed only of carbon and hydrogen atoms, which can include fused or bridged ring systems, having three to twenty carbon atoms, preferably having three to ten carbon atoms, and is attached to the other part of the molecule by a single bond. Monocyclic cycloalkyl radicals include, for example, cyclopropyl, cyclobutyl, cyclopentyl, cyclohexyl, cycloheptyl, and cyclooctyl. Polycyclic cycloalkyl radicals include, for example, adamantyl, nor bornyl, decahydronaphthyl, 7,7-dimethyl-bicyclo[2.2.1]heptyl, and the like. Unless otherwise specifically stated in the specification, the cycloalkyl can be optionally substituted. "Cycloalkenyl" refers to a stable non-aromatic monocyclic or polycyclic hydrocarbon radical composed only of carbon and hydrogen atoms, which has one or more carbon-carbon double bonds, can include fused or bridged ring systems, having three to twenty carbon atoms, preferably having three to ten carbon atoms, and is attached to the other part of the molecule by a single bond. Monocyclic cycloalkenyl radicals include, for example, cyclopentenyl, cyclohexenyl, cycloheptenyl, cyclooctenyl, and the like. Polycyclic cycloalkenyl radicals include, for example, bicyclo[2.2.1]hept-2-enyl and the like. Unless otherwise specifically stated in the specification, the cycloalkenyl can be optionally substituted. "Cycloalkynyl" refers to a stable non-aromatic monocyclic or polycyclic hydrocarbon radical composed only of carbon and hydrogen atoms, having one or more carbon-carbon triple bonds, optionally including fused or bridged ring systems, having from three to twenty carbon atoms, preferably from three to ten carbon atoms, and being attached to the rest of the molecule by a single bond. Monocyclic cycloalkynyl radicals include, for example, cycloheptynyl, cyclooctynyl, and the like. Unless otherwise specifically stated in the specification, cycloalkynyl may be optionally substituted. "Heterocyclyl", "heterocyclic ring" or "heterocycle" refers to a stable 3- to 20-membered non-aromatic ring radical composed of two to twelve carbon atoms and one to six heteroatoms selected from the group consisting of nitrogen, oxygen, and sulfur. Heterocyclyl or heterocycle includes heteroaryl as defined hereinafter. Unless otherwise specifically stated in the specification, heterocyclyl radicals may be monocyclic, bicyclic, tricyclic, or tetracyclic ring systems, which may include fused or bridged ring systems; and the nitrogen, carbon, or sulfur atoms in the heterocyclyl radicals may be optionally oxidized; the nitrogen atoms may be optionally quaternized; and the heterocyclyl radicals may be partially or fully saturated. Examples of such heterocyclyl radicals include, but are not limited to, dioxolanyl, thienyl[1,3]dithianyl, decahydroisoquinolinyl, imidazolinyl, imidazolidinyl, isothiazolidinyl, iso oxazolidinyl, pyrrolinyl, octahydroindolyl, octahydroisoindolyl, 2-oxopiper idinyl, 2-oxopiperidinyl, 2-oxopyrrolidinyl, oxazolidinyl, piperidinyl, piper idinyl, 4-piperidone, pyrrolidinyl, pyrazolidinyl, pyridinyl, tetrahydrothiazolyl, tetrahydrofuranyl, trithianyl, tetrahydropyranyl, thio morpholinyl, thia morpholinyl, 1-oxo-thio morpholinyl, and 1,1-dioxo-thio morpholinyl. Unless otherwise specifically stated in the specification, heterocyclyl may be optionally substituted. "Heteroaryl" refers to a 5- to 20-membered ring system radical containing hydrogen atoms, one to thirteen carbon atoms, one to six heteroatoms selected from the group consisting of nitrogen, oxygen, and sulfur, and at least one aromatic ring. For the purposes of the present invention, heteroaryl radicals may be monocyclic, bicyclic, tricyclic, or tetracyclic ring systems, which may include fused or bridged ring systems; and the nitrogen, carbon, or sulfur atoms in the heteroaryl radicals may be optionally oxidized; the nitrogen atoms may be optionally quaternized. Examples include, but are not limited to, azepinyl, acridinyl, benzimidazolyl, benzothiazolyl, benzindolyl, benzod Uh-yl, benzofuranyl, benzo oxazolyl, benzothiazolyl, benzothiadiazolyl, benzo[ b] [1,4] dioxolane, 1,4-benzodioxadiazole Alkyl, benzonaphthofuranyl, benzo Azolyl, benzophenone benzophenone, benzothiophene, benzotriazolyl, benzo[4,6]imidazo[1,2-a]pyridinyl, carbazolyl, phenanthroline, dibenzofuranyl, dibenzophenylthio, furanyl, furanonyl, isothiazolyl, imidazolyl, indazolyl, indolyl, indazolyl, isoindolyl, indolinyl, isoindololinyl, isoquinolinyl, indole Base, foreign Azolyl, Pyridyl, Oxazolyl, 2-oxo-nitrogen phenyl, oxazolyl, oxirane, 1-oxo-pyridinyl, 1-oxo-pyrimidinyl, 1-oxo-pyrimidinyl 1-oxo-bridged 1-phenyl-1 H-pyrrolyl, phenanthroline Phenylthiophene Base, coffee Base, tie pyrrolyl, pyrazolyl, pyridinyl, pyridinyl pyrimidine, pyrimidine Quinazolinyl, quinazolinyl Phyllinyl, quinolinyl, pyridyl, isoquinolyl, tetrahydroquinolyl, thiazolyl, thiadiazolyl, triazolyl, tetrazolyl, tri Unless otherwise specifically stated in the specification, a heteroaryl group may be optionally substituted. As used herein, the term "substituted" means that at least one hydrogen atom in any of the above groups (i.e., alkyl, alkenyl, alkynyl, cycloalkyl, cycloalkenyl, cycloalkynyl, heterocyclic group, aryl, heteroaryl, alkoxy, aryloxy, acyl, alkylcarbamoyl, alkylcarboxamide, alkoxycarbonyl, alkylthio, or arylthio) is replaced by a bond to a non-hydrogen atom, such as, but not limited to: a halogen atom such as F, Cl, Br, and I; an oxygen atom in a group such as a hydroxyl, alkoxy, and ester group; a sulfur atom in a group such as a mercapto, thioalkyl, sulfone group, sulfonyl group, and sulfoxide group; a nitrogen atom in a group such as an amine, amide, alkylamine, dialkylamine, arylamine, alkylarylamine, diarylamine, N-oxide, imide, and enamine; a silicon atom in a group such as a trialkylsilyl, dialkylarylsilyl, alkyldiarylsilyl, and triarylsilyl group; and other heteroatoms in various other groups. "Substituted" also means any of the above groups in which one or more hydrogen atoms are replaced by a higher order bond (e.g., a double bond or a triple bond) to a heteroatom, such as oxygen in a side-oxy, carbonyl, carboxyl, and ester group; and nitrogen in a group such as an imine, oxime, hydrazone, and nitrile. For example, "substituted" includes those in which one or more hydrogen atoms are replaced by -NR g R h 、-NR g C(=O)R h 、-NR g C(=O)NR g R h 、-NR g C(=O)OR h 、-NR g SO 2 R h 、-OC(=O)NR g R h 、-OR g 、-SR g 、-SOR g 、-SO 2 R g 、 -OSO 2 R g 、 -SO 2 OR g 、 =NSO 2 R g 、及 -SO 2 NR g R h Any of the above groups as substituted. "Substituted" also means that one or more hydrogen atoms are replaced by -C(=O)R g 、 -C(=O)OR g 、 -C(=O)NR g R h 、 -CH 2 SO 2 R g 、 -CH 2 SO 2 NR g R h Any of the above groups as substituted. In the foregoing, R g 及R h are the same or different and independently are hydrogen, alkyl, alkenyl, alkynyl, alkoxy, alkylamino, thioalkyl, aryl, aralkyl, cycloalkyl, cycloalkenyl, cycloalkynyl, cycloalkylalkyl, haloalkyl, haloalkenyl, haloalkynyl, heterocyclic group, N - heterocyclic group, heterocycloalkyl, heteroaryl, N-heteroaryl and / or heteroarylalkyl. "Substituted" further means that one or more hydrogen atoms are attached to an amino group, a cyano group, a hydroxyl group, an imino group, a nitro group, a side oxygen group, a thioketone group, a halogen group, an alkyl group, an alkenyl group, an alkynyl group, an alkoxy group, an alkylamino group, a thioalkyl group, an aryl group, an aralkyl group, a cycloalkyl group, a cycloalkenyl group, a cycloalkynyl group, a cycloalkylalkyl group, a haloalkyl group, a haloalkenyl group, a haloalkynyl group, a heterocyclic group, N-heterocyclic group, heterocycloalkyl group, heteroaryl group, any of the above groups in which the bonding substitution of N-heteroaryl and / or heteroarylalkyl. In addition, each of the foregoing substituents may also be optionally substituted with one or more of the above substituents. Cell penetrating peptide Compounds having activity such as cell penetrating peptides (CPPs) are disclosed herein. In some embodiments, the CPP includes any combination between two or three arginines and at least two hydrophobic amino acids, and the total number of amino acids in the CPP ranges from 4 to about 20 amino acids. In some embodiments, the CPPs disclosed herein contain from about 4 to about 13 amino acids, such as about 5, about 6, about 7, about 8, about 9, about 10, or about 11 amino acids, or about 12 amino acids, including all ranges and subranges therebetween. In a specific embodiment, the CPPs disclosed herein contain from about 6 to about 10 amino acids, or from about 6 to about 8 amino acids. Each amino acid can be a natural or non-natural amino acid. The term "non-natural amino acid" refers to an organic compound that is a homolog of a natural amino acid and has a structure similar to that of a natural amino acid so as to mimic the structure and reactivity of a natural amino acid. Non-natural amino acids can be modified amino acids and / or amino acid analogs that are not one of the 20 common naturally occurring amino acids or the rare natural amino acids selenocysteine or pyrrolysine. Non-natural amino acids can also be D-isomers of natural amino acids. Thus, as used herein, the term "amino acid" refers to natural and non-natural amino acids, and their analogs and derivatives. Examples of suitable amino acids include, but are not limited to, alanine, alloisoleucine, arginine, asparagine, aspartic acid, cysteine, glutamine, glutamic acid, glycine, histidine, isoleucine, leucine, lysine, methionine, naphthylalanine, phenylalanine, proline, pyroglutamic acid, serine, threonine, tryptophan, tyrosine, valine, derivatives, or combinations thereof. These and others, along with their abbreviations used herein, are listed in Table 1. Table 1. Amino acid abbreviations * Single-letter abbreviation: When shown in uppercase letters herein, it indicates the L-amino acid form, and when shown in lowercase letters herein, it indicates the D-amino acid form. In some embodiments, the present disclosure provides a cyclic peptide having a structure according to Formula I: wherein: AA 1 , AA 2 , AA 3 , AA 4 , AA 5 , and AA 6 each of which is independently selected from amino acids; and AA 7 , AA 8 , AA 9 , and AA 10 each of which is independently absent or selected from amino acids; and wherein: AA 1 , AA 2 , AA 3 , AA 4 , AA 5 , AA 6 , AA 7 , AA 8 , AA 9 , or AA 10 two or three of which are arginine, and the remaining amino acids are amino acids other than arginine; and AA 1 , AA 2 , AA 3 , AA 4 , AA 5 , AA 6 , AA 7 , AA 8 , AA 9 , or AA 10 At least two of them are independently hydrophobic amino acids. The amino acids of formula I and their arrangements are described in detail below. In some embodiments, the CPPs (i.e., cyclic peptides of formula I) disclosed herein have a structure according to any one of formulas I-A to I-E: , , , , or where AA 1 , AA 2 , AA 3 , AA 4 , AA 5 , AA 6 , AA 7 , AA 8 , AA 9 , and AA 10 Each of them, when present, is independently selected from amino acids; and where: AA 1 , AA 2 , AA 3 , AA 4 , AA 5 , AA 6 , AA 7 , AA 8 , AA 9 , or AA 10 Two or three of them, when present, are arginine, and the remaining amino acids are amino acids other than arginine; and AA 1 , AA 2 , AA 3 , AA 4 , AA 5 , AA 6 , AA 7 , AA 8 , AA 9 , or AA 10 When at least two of them are present, they are independently hydrophobic amino acids. When the cyclic peptide has a structure according to Formula I-A, AA 1 , AA 2 , AA 3 , AA 4 , AA 5 , and AA 6 Two or three of them are arginine. When the cyclic peptide has a structure according to Formula I-B, AA 1 , AA 2 , AA 3 , AA 4 , AA 5 , AA 6 , and AA 7 Two or three of them are arginine. When the cyclic peptide has a structure according to Formula I-C, AA 1 , AA 2 , AA 3 , AA 4 , AA 5 , AA 6 , AA 7 , and AA 8Two or three of them are arginine. When the cyclic peptide has a structure according to Formula I-D, AA 1 、AA 2 、AA 3 、AA 4 、AA 5 、AA 6 、AA 7 、AA 8 、and AA 9 Two or three of them are arginine. When the cyclic peptide has a structure according to Formula I-E, AA 1 、AA 2 、AA 3 、AA 4 、AA 5 、AA 6 、AA 7 、AA 8 、AA 10 、and AA 10 Two or three of them are arginine. Thus, the cyclic peptide sequences according to Formulas I, I-A, I-B, I-C, I-D, and I-E include two or three arginines, but no more than three arginines. In some embodiments, each hydrophobic amino acid is independently selected from glycine, alanine, valine, leucine, isoleucine, methionine, phenylalanine, tryptophan, proline, naphthylalanine, phenylglycine, homo-phenylalanine, tyrosine, cyclohexylalanine, piperidine-2-carboxylate, 3-(3-benzothienyl)-alanine, or norleucine, each of which is optionally substituted with one or more substituents. In a specific embodiment, each hydrophobic amino acid is independently a hydrophobic aromatic amino acid. In some embodiments, the aromatic hydrophobic amino acids are naphthylalanine, phenylglycine, homo-phenylalanine, phenylalanine, tryptophan, 3-(3-benzothienyl)-alanine, 3-(2-quinolyl)-alanine, O-benzylserine, 3-(4-(benzyloxy)phenyl)-alanine, S-(4-methylbenzyl)cysteine, N-(naphthalen-2-yl)glutamic acid, 3-(1,1'-biphenyl-4-yl)-alanine, 3-(3-benzothienyl)-alanine, or tyrosine, each of which is optionally substituted with one or more substituents. Several structures of these non-natural aromatic hydrophobic amino acids (before incorporation into the peptides disclosed herein) are provided below. In a specific embodiment, the hydrophobic amino acid is piperidine-2-carboxylate, naphthylalanine, tryptophan, 3-(3-benzothienyl)-alanine, or phenylalanine, each of which is optionally substituted with one or more substituents. , , , , , , . Those of ordinary skill in the art will understand that the N-terminus and / or C-terminus of the above non-natural aromatic hydrophobic amino acids form amide linkages when incorporated into the peptides disclosed herein (such as the peptides of Formula I, I-A to I-E, II-A to II-D, III-A to III-D, IV-A to IV-P, and V-A to V-D). Optional substituents can be any atom or group that does not significantly reduce the cytosolic delivery efficiency of the CPP, such as a substituent that does not reduce the relative cytosolic delivery efficiency to less than the relative cytosolic delivery efficiency of c(FФRRRRQ) (SEQ ID NO:10). In some embodiments, the optional substituent can be a hydrophobic substituent or a hydrophilic substituent. In certain embodiments, the optional substituent is a hydrophobic substituent. In some embodiments, the substituent increases the solvent-accessible surface area of the hydrophobic amino acid (as defined hereinbelow). In some embodiments, the substituent can be a halogen, alkyl, alkenyl, alkynyl, cycloalkyl, cycloalkenyl, cycloalkynyl, heterocyclic group, aryl, heteroaryl, alkoxy, aryloxy, acyl, alkylaminocarbonyl, alkylcarboxamide, alkoxycarbonyl, alkylthio, or arylthio. In some embodiments, the substituent is a halogen. Amino acids with relatively high hydrophobicity values can be selected to improve the cytoplasmic delivery efficiency relative to amino acids with lower hydrophobicity values. In some embodiments, each hydrophobic amino acid independently has a hydrophobicity value greater than that of glycine. In other embodiments, each hydrophobic amino acid is independently a hydrophobic amino acid having a hydrophobicity value greater than that of alanine. In still other embodiments, each hydrophobic amino acid independently has a hydrophobicity value greater than or equal to that of phenylalanine. Hydrophobicity can be measured using hydrophobicity scales known in the art. Table 2 below lists the hydrophobicity values of various amino acids reported by Eisenberg and Weiss (Proc. Natl. Acad. Sci. U. S. A. 1984; 81(1):140–144), Engleman, et al. (Ann. Rev. of Biophys. Biophys. Chem.. 1986; 1986(15):321–53), Kyte and Doolittle (J. Mol. Biol. 1982; 157(1):105–132), Hoop and Woods (Proc. Natl. Acad. Sci. U. S. A. 1981; 78(6):3824–3828), and Janin (Nature. 1979; 277(5696):491–492), each of which is incorporated herein by reference in its entirety. In a specific embodiment, hydrophobicity is measured using the hydrophobicity scale reported by Engleman et al. Table 2. The chirality of the amino acids can be selected to improve cytoplasmic uptake efficiency. In some embodiments, at least two of the amino acids have relative chirality. In some embodiments, at least two amino acids having relative chirality can be adjacent to each other. In some embodiments, at least three amino acids have alternating chirality relative to each other. In some embodiments, at least three amino acids having alternating chirality relative to each other can be adjacent to each other. In some embodiments, at least two of the amino acids have the same chirality. In some embodiments, at least two amino acids having the same chirality can be adjacent to each other. In some embodiments, at least two adjacent amino acids have the same chirality and at least two adjacent amino acids have relative chirality. In some embodiments, at least two amino acids having relative chirality can be adjacent to at least two amino acids having the same chirality. Thus, in some embodiments, adjacent amino acids in the CPP can have any of the following sequences: D-L; L-D; D-L-L-D; L-D-D-L; L-D-L-L-D; D-L-D-D-L; D-L-L-D-L; or L-D-D-L-D. In some embodiments, arginine is adjacent to a hydrophobic amino acid. In some embodiments, arginine has the same chirality as the hydrophobic amino acid. In some embodiments, at least two arginines are adjacent to each other. In other embodiments, three arginines are adjacent to each other. In some embodiments, at least two hydrophobic amino acids are adjacent to each other. In other embodiments, at least three hydrophobic amino acids are adjacent to each other. In other embodiments, the CPPs described herein comprise at least two consecutive hydrophobic amino acids and at least two consecutive arginines. In further embodiments, one hydrophobic amino acid is adjacent to one of the arginines. In still other embodiments, the CPPs described herein comprise at least three consecutive hydrophobic amino acids and three consecutive arginines. In further embodiments, one hydrophobic amino acid is adjacent to one of the arginines. The various combinations of these amino acids can have any arrangement of D and L amino acids, such as any of the sequences described in the preceding paragraphs. In some embodiments, any four adjacent amino acids in the CPPs described herein (e.g., CPPs according to Formulas IA to I-D) can have one of the following sequences: AA H2 -AA H1 -R-r, AA H2 -AA H1 -r-R, R-r-AA H1 -AA H2 、or r-R-AA H1 -AA H2 ,where AA H1 and AA H2 each independently is a hydrophobic amino acid. Thus, in some embodiments, the CPPs described herein have a structure according to any one of Formulas II-A to II-D: 、 、and where: AA H1 and AA H2 each independently is a hydrophobic amino acid; AA U and AA Z each independently is any amino acid each time it appears; and each AA U and each AA Z at most one of them is arginine; and wherein: each of m and n is independently a number from 0 to 6, provided that at least one of m or n is not 0 and the total number of amino acids is from 6 to 10. In some embodiments, the amino acids in the CPPs of Formulas II-A to II-D (including r, R, AA H1 、AA H2 ) the total number is in the range of 6 to 10. In some embodiments, the total number of amino acids is 6. In some embodiments, the total number of amino acids is 7. In some embodiments, the total number of amino acids is 8. In some embodiments, the total number of amino acids is 9. In some embodiments, the total number of amino acids is 10. In some embodiments, the sum of m and n is from 2 to 6. In some embodiments, the sum of m and n is 2. In some embodiments, the sum of m and n is 3. In some embodiments, the sum of m and n is 4. In some embodiments, the sum of m and n is 5. In some embodiments, the sum of m and n is 6. In some embodiments, m is 0. In some embodiments, m is 1. In some embodiments, m is 2. In some embodiments, m is 3. In some embodiments, m is 4. In some embodiments, m is 5. In some embodiments, m is 6. In some embodiments, n is 0. In some embodiments, n is 1. In some embodiments, n is 2. In some embodiments, n is 3. In some embodiments, n is 4. In some embodiments, n is 5. In some embodiments, n is 6. In some embodiments, each hydrophobic amino acid is independently selected from glycine, alanine, valine, leucine, isoleucine, methionine, phenylalanine, tryptophan, proline, naphthylalanine, phenylglycine, homo-phenylalanine, tyrosine, cyclohexylalanine, piperidine-2-carboxylate, or norleucine, each of which is optionally substituted with one or more substituents. In a specific embodiment, each hydrophobic amino acid is independently a hydrophobic aromatic amino acid. In some embodiments, the aromatic hydrophobic amino acid is naphthylalanine, phenylglycine, homo-phenylalanine, phenylalanine, tryptophan, 3-(3-benzothienyl)-alanine, 3-(2-quinolyl)-alanine, O-benzylserine, 3-(4-(benzyloxy)phenyl)-alanine, S-(4-methylbenzyl)cysteine, N-(naphthalen-2-yl)glutamic acid, 3-(1,1'-biphenyl-4-yl)-alanine, 3-(3-benzothienyl)-alanine, or tyrosine, each of which is optionally substituted with one or more substituents. In a specific embodiment, the hydrophobic amino acid is piperidine-2-carboxylate, naphthylalanine, tryptophan, 3-(3-benzothienyl)-alanine, or phenylalanine, each of which is optionally substituted with one or more substituents. In some embodiments, AA H1 and AA H2 each independently is a hydrophobic amino acid having a hydrophobicity value greater than that of glycine. In other embodiments, AA H1 and AA H2 each independently is a hydrophobic amino acid having a hydrophobicity value greater than that of alanine. In still other embodiments, AA H1 and AA H2 each independently is a hydrophobic amino acid having a hydrophobicity value greater than that of phenylalanine, such as measured using the hydrophobicity scales described above, including Eisenberg and Weiss (Proc. Natl. Acad. Sci. U. S. A. 1984; 81(1):140–144), Engleman, et al. (Ann. Rev. of Biophys. Biophys. Chem.. 1986; 1986(15):321–53), Kyte and Doolittle (J. Mol. Biol. 1982; 157(1):105–132), Hoop and Woods (Proc. Natl. Acad. Sci. U. S. A. 1981; 78(6):3824–3828), and Janin (Nature. 1979; 277(5696):491–492) (see Table 1 above). In a specific embodiment, the hydrophobicity is measured using the hydrophobicity scale reported by Engleman et al. It has also been found that the presence of a hydrophobic amino acid at the N-terminus or C-terminus of D-Arg or L-Arg, or in combination therewith, improves the cytosolic uptake of CPP (and attached cargo). For example, in some embodiments, the CPPs disclosed herein may include AA H1 -D-Arg or D-Arg-AA H1。In other embodiments, the CPPs disclosed herein may include AA H1 -L-Arg or L-Arg-AA H1 。In some embodiments, the presence of a hydrophobic amino acid at the N-terminus and / or C-terminus of D-Arg or L-Arg in the CPP, or a combination thereof, improves cytosolic delivery efficiency by about 1.1-fold to about 30-fold, such as about 1.2-fold, about 1.3-fold, about 1.4-fold, about 1.5-fold, about 1.6-fold, about 1.7-fold, about 1.8-fold, about 1.9-fold, about 2.0-fold, about 2.5-fold, about 3.0-fold, about 3.5-fold, about 4.0-fold, about 4.5-fold, about 5.0-fold, about 5.5-fold, about 6.0-fold, about 6.5-fold, about 7.0-fold, about 7.5-fold, about 8.0-fold, about 8.5-fold, about 9.0-fold, about 10-fold, about 10.5-fold, about 11.0-fold, about 11.5-fold, about 12.0-fold, about 12.5-fold, about 13.0-fold, about 13.5-fold, about 14.0-fold, about 14.5-fold, about 15.0-fold, about 15.5-fold, about 16.0-fold, about 16.5-fold, about 17.0-fold, about 17.5-fold, about 18.0-fold, about 18.5-fold, about 19.0-fold, about 19.5-fold, about 20-fold, about 20.5-fold, about 21.0-fold, about 21.5-fold, about 22.0-fold, about 22.5-fold, about 23.0-fold, about 23.5-fold, about 24.0-fold, about 24.5-fold, about 25.0-fold, about 25.5-fold, about 26.0-fold, about 26.5-fold, about 27.0-fold, about 27.5-fold, about 28.0-fold, about 28.5-fold, about 29.0-fold, or about 29.5-fold, including all values and sub-ranges therebetween. In some embodiments, the presence of a hydrophobic amino acid at the N-terminus and / or C-terminus of D-Arg and / or L-Arg in the CPP improves cytosolic uptake efficiency by about 20-fold. Optionally, a hydrophobic amino acid at the N-terminus and / or C-terminus of D-Arg or L-Arg, or a combination thereof (i.e., AA H1), to improve the cytoplasmic delivery efficiency of CPP. For example, a larger hydrophobic amino acid at the N-terminus or C-terminus of D-Arg or L-Arg, or a combination thereof, improves cytoplasmic delivery efficiency compared to a sequence with a smaller hydrophobic amino acid otherwise identical. The size of the hydrophobic amino acid can be measured in terms of the molecular weight of the hydrophobic amino acid, the steric effect of the hydrophobic amino acid, the solvent-accessible surface area (SASA) of the side chain, or a combination thereof. In some embodiments, the size of the hydrophobic amino acid is measured in terms of the molecular weight of the hydrophobic amino acid, and the larger hydrophobic amino acid has a side chain with a molecular weight of at least about 90 g / mol, or at least about 130 g / mol, or at least about 141 g / mol. In a specific embodiment, the size of the amino acid is measured in terms of the SASA of the hydrophobic side chain, and the larger hydrophobic amino acid has a side chain with a SASA greater than that of alanine, or greater than that of glycine. In other embodiments, AA H1 has a hydrophobic side chain with a SASA greater than or equal to about piperidine-2-carboxylate, greater than or equal to about tryptophan, greater than or equal to about phenylalanine, or equal to or greater than about naphthylalanine. In some embodiments, AA H1 and AA H2 independently have a side chain with a SASA in the range of about 200 Å 2 to about 1000 Å 2 , for example, about 250 Å 2 , 300 Å 2 , 350 Å 2 , 400 Å 2 , 450 Å 2 , 500 Å 2 , 550 Å 2 , 650 Å 2 , 700 Å 2 , 750 Å 2 , 800 Å 2 , 850 Å 2 , 900 Å 2, and about 950 Å 2 , including all values and sub - ranges therebetween. In some embodiments, AA H1 has a SASA of at least about 200 Å 2 , at least about 210 Å2, at least about 220 Å 2 , at least about 240 Å 2 , at least about 250 Å 2 , at least about 260 Å 2 , at least about 270 Å 2 , at least about 280 Å 2 , at least about 290 Å 2 , at least about 300 Å 2 , at least about 310 Å 2 , at least about 320 Å 2 , or at least about 330 Å 2 of the side chain. In some embodiments, AA H2 has a SASA of at least about 200 Å 2 , at least about 210 Å2, at least about 220 Å 2 , at least about 240 Å 2 , at least about 250 Å 2 , at least about 260 Å 2 , at least about 270 Å 2 , at least about 280 Å 2 , at least about 290 Å 2 , at least about 300 Å 2 , at least about 310 Å 2 , at least about 320 Å 2 or at least about 330 Å 2 side chains. In some embodiments, AA H1 and AA H2 side chains have at least about 350 Å 2 at least about 360 Å 2 at least about 370 Å 2 at least about 380 Å 2 at least about 390 Å 2 at least about 400 Å 2 at least about 410 Å 2 at least about 420 Å 2 at least about 430 Å 2 at least about 440 Å 2 at least about 450 Å 2 at least about 460 Å 2 at least about 470 Å 2 at least about 480 Å 2 at least about 490 Å 2 greater than about 500 Å 2 at least about 510 Å 2 at least about 520 Å 2 at least about 530 Å 2 at least about 540 Å 2 at least about 550 Å 2 at least about 560 Å 2 at least about 570 Å 2 at least about 580 Å 2 , at least about 590 Å 2 , at least about 600 Å 2 , at least about 610 Å 2 , at least about 620 Å 2 , at least about 630 Å 2 , at least about 640 Å 2 , greater than about 650 Å 2 , at least about 660 Å 2 , at least about 670 Å 2 , at least about 680 Å 2 , at least about 690 Å 2 , or at least about 700 Å 2 of the combined SASA. In some embodiments, the AA H2 is the SASA of the side chain is less than or equal to AA H1The SASA of the hydrophobic side chains of hydrophobic amino acids. By way of illustration and not limitation, a CPP having a Nal-Arg motif exhibits improved cytosolic delivery efficiency compared to a CPP having a Phe-Arg motif that is otherwise identical; a CPP having a Phe-Nal-Arg motif exhibits improved cytosolic delivery efficiency compared to a CPP having a Nal-Phe-Arg motif that is otherwise identical; and a phe-Nal-Arg motif exhibits improved cytosolic delivery efficiency compared to a CPP having a nal-Phe-Arg motif that is otherwise identical. In some embodiments, the presence of a larger hydrophobic amino acid at the N-terminus and / or C-terminus of D-Arg or L-Arg in a CPP, or a combination thereof, improves cytosolic delivery efficiency by about 1.1-fold to about 30-fold compared to an otherwise identical sequence, such as about 1.2-fold, about 1.3-fold, about 1.4-fold, about 1.5-fold, about 1.6-fold, about 1.7-fold, about 1.8-fold, about 1.9-fold, about 2.0-fold, about 2.5-fold, about 3.0-fold, about 3.5-fold, about 4.0-fold, about 4.5-fold, about 5.0-fold, about 5.5-fold, about 6.0-fold, about 6.5-fold, about 7.0-fold, about 7.5-fold, about 8.0-fold, about 8.5-fold, about 9.0-fold, about 10-fold, about 10.5-fold, about 11.0-fold, about 11.5-fold, about 12.0-fold, about 12.5-fold, about 13.0-fold, about 13.5-fold, about 14.0-fold, about 14.5-fold, about 15.0-fold, about 15.5-fold, about 16.0-fold, about 16.5-fold, about 17.0-fold, about 17.5-fold, about 18.0-fold, about 18.5-fold, about 19.0-fold, about 19.5-fold, about 20-fold, about 20.5-fold, about 21.0-fold, about 21.5-fold, about 22.0-fold, about 22.5-fold, about 23.0-fold, about 23.5-fold, about 24.0-fold, about 24.5-fold, about 25.0-fold, about 25.5-fold, about 26.0-fold, about 26.5-fold, about 27.0-fold, about 27.5-fold, about 28.0-fold, about 28.5-fold, about 29.0-fold, or about 29.5-fold, including all values and subranges therebetween. In a specific embodiment, the presence of a larger hydrophobic amino acid at the N-terminus and / or C-terminus of D-Arg and / or L-Arg in a CPP improves cytosolic uptake efficiency by about 20-fold. As used herein, "hydrophobic surface area" or "SASA" refers to the surface area of the amino acid side chains accessible to solvent (reported in square angstroms; Å 2 ). In a specific embodiment, SASA is calculated using the "rolling ball" algorithm developed by Shrake & Rupley ( J Mol Biol. Calculated by 79(2): 351–71), the full text of which is incorporated herein by reference for all purposes. This algorithm uses a solvent "sphere" with a specific radius to probe the surface of the molecule. A typical value of the sphere is 1.4 Å, which approximates the radius of a water molecule. The SASA values of certain side chains are shown in Table 3 below. In some embodiments, the SASA values described herein are based on the theoretical values listed in Table 3 below, reported by Tien et al. (PLOS ONE 8(11): e80635. https: / / doi.org / 10.1371 / journal.pone.0080635), the full text of which is incorporated herein by reference for all purposes. Table 3. In some embodiments, the CPP is at the N-terminus and / or C-terminus of AA H2 -AA H1 -R-r, AA H2 -AA H1 -r-R, R-r-AA H1 -AA H2 、or r-R-AA H1 -AA H2 does not include hydrophobic amino acids at the N-terminus and / or C-terminus of. In alternative embodiments, the CPP does not include side chains greater than (as described herein) AA H1 or AA H2 of at least one hydrophobic amino acid. In further embodiments, the CPP does not include hydrophobic amino acids with side chain surface areas greater than AA H1 That is, when any AA U or any AA Z is a hydrophobic amino acid (e.g., in Formulas I, I-A to I-E, II-A to II-D, III-A to III-D, IV-A to IV-P, and V-A to V-D), the SASA of the side chain of the hydrophobic amino acid is less than AA H1 . For example, in AA H1 or AA H2 In embodiments in which at least one of them is phenylalanine, CPP does not further include naphthylalanine (although CPP may include at least one amino acid smaller than AA H1 and AA H2 hydrophobic amino acids such as leucine). In still other embodiments, CPP, in addition to in AA H2 -AA H1 -R-r, AA H2 -AA H1 -r-R, R-r-AA H1 -AA H2 or r-R-AA H1 -AA H2 does not include naphthylalanine (or larger hydrophobic amino acids) other than the hydrophobic amino acids in. The chirality of the amino acid can be selected (i.e., D or L amino acid) to improve the cytoplasmic delivery efficiency of CPP (and the attached cargo as described below). In some embodiments, the hydrophobic amino acid (such as AA H1 on the N-terminus or C-terminus of arginine u or AA z ) has the same or opposite chirality as the adjacent arginine. In some embodiments, AA H1 has the opposite chirality to the adjacent arginine. For example, when arginine is D-arg (i.e., "r"), AA H1 is D-AA H1 , and when arginine is L-Arg (i.e., "R"), AA H1 is L-AA H1 . Thus, in some embodiments, the CPPs disclosed herein may include at least one of the following motifs: D-AA H1 -D-arg, D-arg-D-AA H1 L-AA ​H1 -L-Arg, or L-Arg-LAA H1 。In a specific embodiment, when the arginine is D-arg, AA H1 can be D-pip, D-nal, D-trp, D-bta, or D-phe. In another non-limiting example, when the arginine is L-Arg, AA H1 can be L-Pip, L-Nal, L-Trp, L-Bta, or L-Phe. In some embodiments, the presence of a hydrophobic amino acid with the same chirality as the adjacent arginine improves cytosolic delivery efficiency by about 1.1-fold to about 30-fold compared to an otherwise identical sequence, such as about 1.2-fold, about 1.3-fold, about 1.4-fold, about 1.5-fold, about 1.6-fold, about 1.7-fold, about 1.8-fold, about 1.9-fold, about 2.0-fold, about 2.5-fold, about 3.0-fold, about 3.5-fold, about 4.0-fold, about 4.5-fold, about 5.0-fold, about 5.5-fold, about 6.0-fold, about 6.5-fold, about 7.0-fold, about 7.5-fold, about 8.0-fold, about 8.5-fold, about 9.0-fold, about 10-fold, about 10.5-fold, about 11.0-fold, about 11.5-fold, about 12.0-fold, about 12.5-fold, about 13.0-fold, about 13.5-fold, about 14.0-fold, about 14.5-fold, about 15.0-fold, about 15.5-fold, about 16.0-fold, about 16.5-fold, about 17.0-fold, about 17.5-fold, about 18.0-fold, about 18.5-fold, about 19.0-fold, about 19.5-fold, about 20-fold, about 20.5-fold, about 21.0-fold, about 21.5-fold, about 22.0-fold, about 22.5-fold, about 23.0-fold, about 23.5-fold, about 24.0-fold, about 24.5-fold, about 25.0-fold, about 25.5-fold, about 26.0-fold, about 26.5-fold, about 27.0-fold, about 27.5-fold, about 28.0-fold, about 28.5-fold, about 29.0-fold, or about 29.5-fold, including all values and sub-ranges therebetween. In some embodiments, the presence of a hydrophobic amino acid with the same chirality as the adjacent arginine improves cytosolic uptake efficiency by about 2.5-fold. In some embodiments, the CPPs described herein include three arginines. Thus, in some embodiments, the CPPs described herein include one of the following sequences: AA H2 -AA H1 -R-r-R, AA H2 -AA H1 -R-r-r, AA H2-AA H1 -r-R-R, AA H2 -AA H1 -r-R-r, R-R-r-AA H1 -AA H2 , r-R-r-AA H1 -AA H2 , r-r-R-AA H1 -AA H2 , or R-r-R-AA H1 -AA H2 . In a specific embodiment, the CPP has one of the following sequences: AA H2 -AA H1 -R-r-R, AA H2 -AA H1 -r-R-r, r-R-r-AA H1 -AA H2 , or R-r-R-AA H1 -AA H2 . In some embodiments, AAH 1 and AAH 2 's chirality can be selected as described above, for example, to improve cytoplasmic uptake efficiency, where AAH 1 has the same chirality as the adjacent arginine, and AAH 1 and AAH 2 have opposite chirality. In some embodiments, the CPPs described herein include three hydrophobic amino acids. Thus, in some embodiments, the CPPs described herein include one of the following sequences: AA H3 -AA H2 -AA H1 -Rr、AA H3 -AA H2 -AA H1 -Rr、AA H3 -AA H2 -AA H1 -rR、AA H3 -AA H2 -AA H1 -rR、Rr-AA H1 -AA H2 -AA H3 、Rr-AA H1 -AA H2 -AA H3 、rR-AA H1 -AA H2 -AA H3 , or rR-AA H1 -AA H2 -AA H3 , where AA H3 is any of the hydrophobic amino acids described above, such as piperidine-2-carboxylate, naphthylalanine, tryptophan, 3-(3-benzothienyl)-alanine, or phenylalanine. H1 AA H2 , and AA H3 The chirality of AAH can be selected, for example, as described above, to improve cytosol uptake efficiency, wherein 1has the same chirality as the adjacent arginine, and AA H1 and AA H2 have opposite chirality. In other embodiments, AA H1 、AA H2 、and AA H3 size can be selected as described above, for example, to improve cytosolic uptake efficiency, where AA H3 has a size less than or equal to AA H1 and separately / or AA H2 of the SAS. In some embodiments, AA H1 and AA H2 have the same or opposite chirality. In certain embodiments, AA H1 and AA H2 have opposite chirality. Thus, in some embodiments, the CPPs disclosed herein include at least one of the following sequences: D-AA H2 -L-AA H1 -R-r; L-AA H2 -D-AA H1 -r-R; R-r-D-AA H1 -L-AA H2 ; or r-R-L-AA H1 -D-AA H1 where each of D-AA H1 and D-AA H2 is a hydrophobic amino acid having a D configuration, and each of L-AA H1 and L-AA H2 is a hydrophobic amino acid having an L configuration. In some embodiments, D-AA H1 and D-AA H2 each of which is independently selected from the group consisting of D-pip, D-nal, D-trp, D-bta, and D-phe. In a specific embodiment, D-AA H1 or D-AA H2 is D-nal. In other specific embodiments, D-AA H1 is D-nal. In some embodiments, L-AA H1 and L-AA H2 each of which is independently selected from the group consisting of L-Pip, L-Nal, L-Trp, L-Bta, and L-Phe. In a specific embodiment, L-AA H1 and L-AA H2 each of which is L-Nal. In other specific embodiments, L-AA H1 is L-Nal. In some embodiments, AAs with opposite chirality H1 and AAs H2The presence improves cytosolic delivery efficiency by about 1.1-fold to about 30-fold, such as about 1.2-fold, about 1.3-fold, about 1.4-fold, about 1.5-fold, about 1.6-fold, about 1.7-fold, about 1.8-fold, about 1.9-fold, about 2.0-fold, about 2.5-fold, about 3.0-fold, about 3.5-fold, about 4.0-fold, about 4.5-fold, about 5.0-fold, about 5.5-fold, about 6.0-fold, about 6.5-fold, about 7.0-fold, about 7.5-fold, about 8.0-fold, about 8.5-fold, about 9.0-fold, about 10-fold, about 10.5-fold, about 11.0-fold, about 11.5-fold, about 12.0-fold, about 12.5-fold, about 13.0-fold, about 13.5-fold, about 14.0-fold, about 14.5-fold, about 15.0-fold, about 15.5-fold, about 16.0-fold, about 16.5-fold, about 17.0-fold, about 17.5-fold, about 18.0-fold, about 18.5-fold, about 19.0-fold, about 19.5-fold, about 20-fold, about 20.5-fold, about 21.0-fold, about 21.5-fold, about 22.0-fold, about 22.5-fold, about 23.0-fold, about 23.5-fold, about 24.0-fold, about 24.5-fold, about 25.0-fold, about 25.5-fold, about 26.0-fold, about 26.5-fold, about 27.0-fold, about 27.5-fold, about 28.0-fold, about 28.5-fold, about 29.0-fold, or about 29.5-fold, including all values and sub-ranges therebetween. In some embodiments, the AA having relative chirality H1 and AA H2 The presence improves cytosolic delivery efficiency by about 1.5-fold. As discussed above, the present disclosure provides various modifications of cyclic peptide sequences that can improve cytosolic delivery efficiency. In some embodiments, the improved cytosolic uptake efficiency can be measured by comparing the cytosolic delivery efficiency of a CPP having a modified sequence with an appropriate control sequence. In some embodiments, the control sequence does not include a particular modification (e.g., the matching chirality of R and AA H1 ), and is otherwise identical to the modified sequence. In other embodiments, the control has the following sequence: Cyclic(FФRRRRQ) (SEQ ID NO:10). As used herein, cytosolic delivery efficiency refers to the ability of a CPP to cross the cell membrane and enter the cytosol. In embodiments, the cytosolic delivery efficiency of a CPP is independent of the receptor or cell type. Cytosolic delivery efficiency can refer to absolute cytosolic delivery efficiency or relative cytosolic delivery efficiency. The absolute cytoplasmic delivery efficiency is the ratio of the cytoplasmic concentration of the CPP (or CPP-cargo conjugate) to the concentration of the CPP (or CPP-cargo conjugate) in the growth medium. The relative cytoplasmic delivery efficiency refers to the concentration of the CPP in the cytoplasm compared to the concentration of a control CPP in the cytoplasm. Quantification can be achieved by fluorescently labeling the CPP (e.g., using an FTIC dye) and measuring the fluorescence intensity using techniques well known in the art. In a specific embodiment, the relative cytoplasmic delivery efficiency is determined by comparing: (i) the amount of the CPP of the present invention internalized by a cell type (e.g., HeLa cells) with (ii) the amount of a control CPP internalized by the same cell type. To measure the relative cytoplasmic delivery efficiency, the cell type can be incubated in the presence of the cell-penetrating peptide of the present invention for a specific time period (e.g., 30 minutes, 1 hour, 2 hours, etc.), after which the amount of the CPP internalized by the cells is quantified using methods known in the art such as fluorescence microscopy. Separately, the same concentration of the control CPP is incubated in the presence of the cell type for the same time period, and the amount of the control CPP internalized by the cells is quantified. In other embodiments, the relative cytoplasmic delivery efficiency can be determined by measuring the IC of the CPP with a modified sequence against a target in the cell 50 and comparing the IC of the CPP with the modified sequence 50 to an appropriate control sequence (as described herein). In some embodiments, the relative cytosolic delivery efficiency of the CPPs described herein is in the range of about 50% to about 450% compared to the loop (FФRRRRQ) (SEQ ID NO:10), such as about 60%, about 70%, about 80%, about 90%, about 100%, about 110%, about 120%, about 130%, about 140%, about 150%, about 160%, about 170%, about 180%, about 190%, about 200%, about 210%, about 220%, about 230%, about 240%, about 250%, about 260%, about 270%, about 280%, about 290%, about 300%, about 310%, about 320%, about 330%, about 340%, about 350%, about 360%, about 370%, about 380%, about 390%, about 400%, about 410%, about 420%, about 430%, about 440%, about 450%, about 460%, about 470%, about 480%, about 490%, about 500%, about 510%, about 520%, about 530%, about 540%, about 550%, about 560%, about 570%, about 580%, or about 590%, including all values and sub-ranges therebetween. In other embodiments, the relative cytosolic delivery efficiency of the CPPs described herein is improved by greater than about 600% compared to the loop (FФRRRRQ) (SEQ ID NO:10). In certain embodiments, the CPP comprises FfFRrR (SEQ ID NO:131) such as the loop (FfFRrRQ) (SEQ ID NO:96), and has a relative cytosolic delivery efficiency of 175% to about 250% compared to the loop (FФRRRRQ) (SEQ ID NO:10). In certain embodiments, the CPP comprises fFfrRr (SEQ ID NO:132) such as the loop (fFfrRrQ) (SEQ ID NO:97), and has a relative cytosolic delivery efficiency of about 150% to about 400% compared to the loop (FФRRRRQ) (SEQ ID NO:10). In certain embodiments, the CPP comprises fFfRrR (SEQ ID NO:133) such as the loop (fFfRrRQ) (SEQ ID NO:98), and has a relative cytosolic delivery efficiency of about 75% to about 275% compared to the loop (FФRRRRQ) (SEQ ID NO:10). In certain embodiments, the CPP comprises FfFrRr (SEQ ID NO:134) such as the loop (FfFrRrQ) (SEQ ID NO:99), and has a relative cytosolic delivery efficiency of about 150% to about 250% compared to the loop (FФRRRRQ) (SEQ ID NO:10).In certain embodiments, the CPP comprises fFɸrRr (SEQ ID NO:135) such as the loop (fFɸrRrQ) (SEQ ID NO:100), and has a relative cytosolic delivery efficiency that is improved by about 200% to about 450% compared to the loop (FФRRRRQ) (SEQ ID NO:10). In certain embodiments, the CPP comprises fФfrRr (SEQ ID NO:136) such as the loop (fФfrRrQ) (SEQ ID NO:101), and has a relative cytosolic delivery efficiency that is improved by about 250% to about 450% compared to the loop (FФRRRRQ) (SEQ ID NO:10). In other embodiments, the absolute cytosolic delivery efficiency is about 40% to about 100%, such as about 45%, about 50%, about 55%, about 60%, about 65%, about 70%, about 75%, about 80%, about 85%, about 90%, about 91%, about 92%, about 93%, about 94%, about 95%, about 96%, about 97%, about 98%, about 99%, including all values and sub-ranges therebetween. In certain embodiments, the CPP is the loop (FfFRrRQ) (SEQ ID NO:96) and has an absolute cytosolic delivery efficiency of 40% to about 50%. In certain embodiments, the CPP is the loop (fFfrRrQ) (SEQ ID NO:97) and has an absolute cytosolic delivery efficiency of about 50% to about 70%. In certain embodiments, the CPP is the loop (fFfRrRQ) (SEQ ID NO:98) and has an absolute cytosolic delivery efficiency of about 30% to about 60%. In certain embodiments, the CPP is the loop (FfFrRrQ) (SEQ ID NO:99) and has an absolute cytosolic delivery efficiency of about 40% to about 55%. In certain embodiments, the CPP is the loop (fFɸrRrQ) (SEQ ID NO:100) and has an absolute cytosolic delivery efficiency of about 55% to about 75%. In certain embodiments, the CPP is the loop (fФfrRrQ) (SEQ ID NO:101) and has an absolute cytosolic delivery efficiency of about 60% to about 80%. In some embodiments, the CPPs (such as those of Formulas I, I-A to I-E, II-A to II-D, III-A to III-D, IV-A to IV-P, and V-A to V-D) disclosed herein are selected from the sequences provided in Table 4 below. Table 4. a Φ, L-2-naphthylalanine; ɸ, D-2-naphthylalanine; f, D-phenylalanine; r, D-arginine; X, L-4-fluorophenylalanine; Dap, L-2,3-diaminopropionic acid. b All values are relative to the value of CPP 1 (100%) and represent the mean ± S.D. of three independent experiments. In some embodiments, the CPP sequences disclosed herein (i.e., the sequences according to Formulas I, I-A to I-E, II-A to II-D, III-A to III-D, IV-A to IV-P, and V-A to V-D) do not include the sequences disclosed in PCT / US2015 / 032043, such as SEQ ID NO:10 c(F ΦRRRRQ); SEQ ID NO:138 c(Ff ΦRrRrQ); SEQ ID NO:94c(f ΦRrRrQ); SEQ ID NO:121 c(f ΦRrRrRQ); SEQ ID NO:122c(FɸrRrRq); SEQ ID NO:123c(FɸrRrRQ); SEQ ID NO:124c(F ΦRRRRRQ); SEQ ID NO:125 c(RRFR ΦRQ); SEQ ID NO:126 c(FF ΦRRRRQ); SEQ ID NO:127 c(RFRFR ΦRQ); SEQ ID NO:128 c(F ΦRRRQ); SEQ ID NO:129 c(FRRRR ΦQ); SEQ ID NO:130 c(rRFR ΦRQ); or SEQ ID NO:137 c(RR ΦFRRQ). Goods In some embodiments, the CPPs disclosed herein may further include a cargo portion, which may comprise a peptide (「X n”). The cargo portion may include one or more detectable portions, one or more therapeutic portions, one or more targeting portions, or any combination thereof. In some embodiments, the cargo portion may be a peptide sequence or a non-peptidyl therapeutic agent. In some embodiments, the cargo portion may be coupled to an amine group (e.g., N-terminus), a carboxylate group (e.g., C-terminus), or a side chain of one or more amino acids in the CPP. In some embodiments, the CPP and the cargo portion together are cyclic (referred to herein as “endocyclic”). In some embodiments, the CPP is cyclic and the cargo portion is attached to the cyclic cell-penetrating peptide portion structure (referred to herein as “exocyclic”). In some embodiments, the cargo portion is cyclic and the CPP is cyclic, and together they form a bicyclic system (referred to herein as “bicyclic”). In certain embodiments, at least one bond in the CPP (e.g., an amide bond between amino acids) is linked to X n to form an endocyclic CPP and a cargo portion. In certain embodiments, X n is coupled to the side chain of an amino acid in the CPP (e.g., cysteine, lysine, glutamic acid, or aspartic acid, or analogs thereof) to form an exocyclic CPP and X n . In certain embodiments, the CPP further includes a linker group (“L”), and X n is attached to the linker group to form a bicyclic CPP and a cargo portion. In certain embodiments, the CPP further includes a linker group (“L”), and X n is attached to the linker group and the side chain of an amino acid in the CPP to form a bicyclic CPP and a cargo portion. Also disclosed herein is an endocyclic structure where some amino acids in the CPP can also be part of the cargo portion. For example, the peptide penetration portion FNalRR can be formed from FNal and the cargo portion contains two Args. In this case, the two Arg residues perform a dual function. Thus, in some cases, when referring to the peptide penetration portion, the sequence of the cargo portion is considered. In some embodiments, the CPPs disclosed herein have a structure according to one of Formulas III-A to III-D: , , , or where: AA 1 , AA 2 , AA 3 and AA 4 Each of those in is independently selected from amino acids; AA U and AA Z Each occurrence is independently selected from amino acids; each of m and n is a number from 0 to 6, provided that at least one of m or n is not 0; Xn is a cargo moiety comprising a therapeutic moiety, a targeting moiety, a detectable moiety, or a combination thereof; L is a linker moiety; wherein: AA 1 AA 2 AA 3 AA 4 each AA U and each AA Z Two or three of those in are arginine, and the remaining amino acids are amino acids other than arginine; AA 1 AA 2 AA 3 AA 4 each AA U and each AA Z At least two of those in are independently hydrophobic amino acids each time they occur; and wherein when X n is attached to AA U m is not 0; In some embodiments, AA 1 AA 2 AA 3 AA 4 Each of those in is independently selected from natural or non-natural amino acids, such as but not limited to those described in Table 1 above. In some embodiments, AA U AA Z Each of those in is independently selected from amino acids, such as but not limited to those described in Table 1 above. In some embodiments, AA 1 、AA 2 、AA 3 、AA 4 、each AA U 、and each AA Z among at least two of them are independently hydrophobic amino acids. In some embodiments, each hydrophobic amino acid is independently selected from glycine, alanine, valine, leucine, isoleucine, methionine, phenylalanine, tryptophan, proline, naphthylalanine, phenylglycine, homo-phenylalanine, tyrosine, cyclohexylalanine, piperidine-2-carboxylate, 3-(3-benzothienyl)-alanine, or norleucine, each of which is optionally substituted with one or more substituents. In a specific embodiment, each hydrophobic amino acid is independently a hydrophobic aromatic amino acid. In some embodiments, the aromatic hydrophobic amino acids are naphthylalanine, phenylglycine, homo-phenylalanine, phenylalanine, tryptophan, 3-(3-benzothienyl)-alanine, 3-(2-quinolyl)-alanine, O-benzylserine, 3-(4-(benzyloxy)phenyl)-alanine, S-(4-methylbenzyl)cysteine, N-(naphthalen-2-yl)glutamic acid, 3-(1,1'-biphenyl-4-yl)-alanine, 3-(3-benzothienyl)-alanine or tyrosine, each of which is optionally substituted with one or more substituents. In a specific embodiment, the hydrophobic amino acid is piperidine-2-carboxylate, naphthylalanine, tryptophan, 3-(3-benzothienyl)-alanine, or phenylalanine, each of which is optionally substituted with one or more substituents. As described above, the optional substituents can be any atom or group that does not significantly reduce the cytosolic delivery efficiency of the CPP, such as a substituent that does not reduce the relative cytosolic delivery efficiency to less than the relative cytosolic delivery efficiency of SEQ ID NO:10 c(FФRRRRQ). In some embodiments, the optional substituents can be hydrophobic substituents or hydrophilic substituents. In certain embodiments, the optional substituents are hydrophobic substituents. In some embodiments, the substituents increase the solvent-accessible surface area of the hydrophobic amino acid (as defined herein). In some embodiments, the substituents can be halogen, alkyl, alkenyl, alkynyl, cycloalkyl, cycloalkenyl, cycloalkynyl, heterocyclic group, aryl, heteroaryl, alkoxy, aryloxy, acyl, alkylaminocarbonyl, alkylcarboxamide group, alkoxycarbonyl, alkylthio, or arylthio. In some embodiments, the substituents are halogen. As discussed above, amino acids with higher hydrophobicity values can be selected to improve the cytoplasmic delivery efficiency relative to amino acids with lower hydrophobicity values. In some embodiments, each hydrophobic amino acid independently has a hydrophobicity value greater than that of glycine. In other embodiments, each hydrophobic amino acid independently has a hydrophobicity value greater than that of alanine (see Table 2 above). In still other embodiments, each hydrophobic amino acid independently has a hydrophobicity value greater than or equal to that of phenylalanine (see Table 2 above). As discussed above, the chirality of the amino acids can be selected to improve cytoplasmic uptake efficiency. In some embodiments, at least two of the amino acids have relative chirality. In some embodiments, at least two amino acids having relative chirality can be adjacent to each other. In some embodiments, at least three amino acids have stereochemistry that alternates relative to each other. In some embodiments, at least three amino acids having alternating chirality relative to each other can be adjacent to each other. In some embodiments, at least two of the amino acids have the same chirality. In some embodiments, at least two amino acids having the same chirality can be adjacent to each other. In some embodiments, at least two amino acids have the same chirality and at least two amino acids have relative chirality. In some embodiments, at least two amino acids having relative chirality can be adjacent to at least two amino acids having the same chirality. Thus, in some embodiments, adjacent amino acids in the CPP can have any of the following sequences: D-L; L-D; D-L-L-D; L-D-D-L; L-D-L-L-D; D-L-D-D-L; D-L-L-D-L; or L-D-D-L-D. In some embodiments, arginine is adjacent to a hydrophobic amino acid. In some embodiments, arginine has the same chirality as the hydrophobic amino acid. In some embodiments, at least two arginines are adjacent to each other. In still other embodiments, three arginines are adjacent to each other. In some embodiments, at least two hydrophobic amino acids are adjacent to each other. In other embodiments, at least three hydrophobic amino acids are adjacent to each other. In other embodiments, the CPPs described herein comprise at least two consecutive hydrophobic amino acids and at least two consecutive arginines. In a further embodiment, one hydrophobic amino acid is adjacent to one of the arginines. In still other embodiments, the CPPs described herein comprise at least three consecutive hydrophobic amino acids and three consecutive arginines. In a further embodiment, one hydrophobic amino acid is adjacent to one of the arginines. The various combinations of these amino acids can have any arrangement of D and L amino acids, such as the sequences described above. In some embodiments, the sum of m and n is from 2 to 6. In some embodiments, the sum of m and n is 2. In some embodiments, the sum of m and n is 3. In some embodiments, the sum of m and n is 4. In some embodiments, the sum of m and n is 5. In some embodiments, the sum of m and n is 6. In some embodiments, m is 0. In some embodiments, m is 1. In some embodiments, m is 2. In some embodiments, m is 3. In some embodiments, m is 4. In some embodiments, m is 5. In some embodiments, m is 6. In some embodiments, n is 0. In some embodiments, n is 1. In some embodiments, n is 2. In some embodiments, n is 3. In some embodiments, n is 4. In some embodiments, n is 5. In some embodiments, n is 6. In some embodiments, the linker (「L」) can be any moiety capable of forming two peptide bonds and also containing at least one functional group suitable for attaching a cargo moiety (X n ). In some embodiments, the linker can be one or more natural or unnatural amino acids. Non-limiting examples of natural amino acids that can serve as linkers are glutamic acid, lysine, and cysteine, and their analogs. In certain embodiments, the linker has one functional group for attaching the cargo moiety, and the cargo moiety is also attached to the side chain of an amino acid (such as glutamic acid, aspartic acid, 2,3-diaminopropionic acid, or lysine, or their analogs) in the CPP to form the second ring of a bicyclic system. In some embodiments, the linker contains at least two functional groups for attaching the cargo moiety. In some embodiments, the linker can have the following structure before being incorporated into the CPP , where each bond connected to the -OH group is independently replaced by a peptide bond connecting to the amino group of the CPP or the cargo. In other embodiments, the linker can have one of the following structures before being incorporated into the CPP: or where each bond connected to the -OH group is independently replaced by a peptide bond connecting to the amino group of the CPP, and each thioether bond between the aryl and sulfur is independently replaced by a disulfide bond with the cargo and optionally with the CPP, provided that each of the cargo and the CPP independently includes cysteine or other unnatural amino acids containing a thiol group, such as those disclosed in U.S. Provisional Patent Application No. 62 / 438,141. In some embodiments, Xn is the cargo moiety (as described above), which includes a therapeutic moiety, a targeting moiety, a detectable moiety, or a combination thereof. Non-limiting examples of therapeutic moieties, targeting moieties, and detectable moieties that can be attached to the CPPs described herein are described below. In some embodiments, the cyclic peptides described herein (e.g., according to Formulas III-A to III-D) have structures according to Formulas IV-A to IV-P: , , , , , , , , , , , , , , , or , wherein: each AAu and AAz is independently any amino acid, e.g., AA as defined above with respect to Formulas III-A to III-D U either each occurrence of or AA Z either each occurrence of; AA H1 and AA H2 each of which is independently a hydrophobic amino acid; and and each AA U and each AA Z at most one of each is arginine; each of m and n is independently a number from 0 to 6, provided that at least one of m or n is not 0 and the total number of amino acids is from 6 to 10. In some embodiments, the total number of amino acids in the CPPs of Formulas IV-A to IV-P (including r, R, AA H1 , AA H2 ) is in the range of 6 to 10. In some embodiments, the total number of amino acids is 6. In some embodiments, the total number of amino acids is 7. In some embodiments, the total number of amino acids is 8. In some embodiments, the total number of amino acids is 9. In some embodiments, the total number of amino acids is 10. In some embodiments, the sum of m and n is from 2 to 6. In some embodiments, the sum of m and n is 2. In some embodiments, the sum of m and n is 3. In some embodiments, the sum of m and n is 4. In some embodiments, the sum of m and n is 5. In some embodiments, the sum of m and n is 6. In some embodiments, m is 0. In some embodiments, m is 1. In some embodiments, m is 2. In some embodiments, m is 3. In some embodiments, m is 4. In some embodiments, m is 5. In some embodiments, m is 6. In some embodiments, n is 0. In some embodiments, n is 1. In some embodiments, n is 2. In some embodiments, n is 3. In some embodiments, n is 4. In some embodiments, n is 5. In some embodiments, n is 6. In some embodiments, AA H1 and AA H2 each independently is a hydrophobic amino acid having a hydrophobicity value greater than that of glycine. In other embodiments, AA H1 and AA H2 each independently is a hydrophobic amino acid having a hydrophobicity value greater than that of alanine. In still other embodiments, AA H1 and AA H2 each independently is a hydrophobic amino acid having a hydrophobicity value greater than that of phenylalanine, such as measured using the hydrophobicity scales described above, including Eisenberg and Weiss (Proc. Natl. Acad. Sci. U. S. A. 1984; 81(1):140–144), Engleman, et al. (Ann. Rev. of Biophys. Biophys. Chem.. 1986; 1986(15):321–53), Kyte and Doolittle (J. Mol. Biol. 1982; 157(1):105–132), Hoop and Woods (Proc. Natl. Acad. Sci. U. S. A. 1981; 78(6):3824–3828), and Janin (Nature. 1979; 277(5696):491–492) (see Table 1 above). In a specific embodiment, the hydrophobicity is measured using the hydrophobicity scale reported by Engleman et al. As described above, it has also been found that the presence of hydrophobic amino acids at the N-terminus and / or C-terminus of D-Arg or L-Arg, or combinations thereof, improves the cytosolic uptake of CPPs (and attached cargo). For example, in some embodiments, the CPPs disclosed herein may include AA H1 -D-Arg or D-Arg-AA H1 。In other embodiments, the CPPs disclosed herein may include AA H1 -L-Arg or L-Arg-AA H1 。In some embodiments, the presence of hydrophobic amino acids at the N-terminus and / or C-terminus of D-Arg or L-Arg, or combinations thereof, in a CPP improves cytosolic delivery efficiency by about 1.1-fold to about 30-fold, such as about 1.2-fold, about 1.3-fold, about 1.4-fold, about 1.5-fold, about 1.6-fold, about 1.7-fold, about 1.8-fold, about 1.9-fold, about 2.0-fold, about 2.5-fold, about 3.0-fold, about 3.5-fold, about 4.0-fold, about 4.5-fold, about 5.0-fold, about 5.5-fold, about 6.0-fold, about 6.5-fold, about 7.0-fold, about 7.5-fold, about 8.0-fold, about 8.5-fold, about 9.0-fold, about 10-fold, about 10.5-fold, about 11.0-fold, about 11.5-fold, about 12.0-fold, about 12.5-fold, about 13.0-fold, about 13.5-fold, about 14.0-fold, about 14.5-fold, about 15.0-fold, about 15.5-fold, about 16.0-fold, about 16.5-fold, about 17.0-fold, about 17.5-fold, about 18.0-fold, about 18.5-fold, about 19.0-fold, about 19.5-fold, about 20-fold, about 20.5-fold, about 21.0-fold, about 21.5-fold, about 22.0-fold, about 22.5-fold, about 23.0-fold, about 23.5-fold, about 24.0-fold, about 24.5-fold, about 25.0-fold, about 25.5-fold, about 26.0-fold, about 26.5-fold, about 27.0-fold, about 27.5-fold, about 28.0-fold, about 28.5-fold, about 29.0-fold, or about 29.5-fold, including all values and subranges therebetween. As discussed above, hydrophobic amino acids (i.e., AA H1), to improve the cytoplasmic delivery efficiency of CPP. For example, a larger hydrophobic amino acid at the N-terminus or C-terminus of D-Arg or L-Arg, or a combination thereof, improves cytoplasmic delivery efficiency compared to a sequence that is otherwise the same but has a smaller hydrophobic amino acid. As discussed above, the size of the hydrophobic amino acid can be measured in terms of the molecular weight of the hydrophobic amino acid, the steric effect of the hydrophobic amino acid, the solvent-accessible surface area (SASA) of the side chain, or a combination thereof. In some embodiments, the size of the hydrophobic amino acid is measured in terms of the molecular weight of the hydrophobic amino acid, and the larger hydrophobic amino acid has a side chain with a molecular weight of at least about 90 g / mol, or at least about 130 g / mol, or at least about 141 g / mol. In other embodiments, the size of the amino acid is measured in terms of the SASA of the hydrophobic side chain, and the larger hydrophobic amino acid has a side chain with a SASA greater than the SASA of alanine, or greater than the SASA of glycine. In other embodiments, AA H1 has a hydrophobic side chain with a SASA greater than or equal to about piperidine-2-carboxylate, greater than or equal to about tryptophan, greater than or equal to about phenylalanine, or equal to or greater than about naphthylalanine. In some embodiments, AA H1 and AA H2 independently have a side chain with a SASA in the range of about 200 Å 2 to about 1000 Å 2 , such as about 250 Å 2 , 300 Å 2 , 350 Å 2 , 400 Å 2 , 450 Å 2 , 500 Å 2 , 550 Å 2 , 650 Å 2 , 700 Å 2 , 750 Å 2 , 800 Å 2 , 850 Å 2 , 900 Å 2 and about 950 Å 2 , including all values and sub-ranges therebetween. In some embodiments, AA H1 has a SASA of at least about 200 Å 2 , at least about 210 Å 2 , at least about 220 Å 2 , at least about 240 Å 2 , at least about 250 Å 2 , at least about 260 Å 2 , at least about 270 Å 2 , at least about 280 Å 2 , at least about 290 Å 2 , at least about 300 Å 2 , at least about 310 Å 2 , at least about 320 Å 2 , or at least about 330 Å 2 side chains. In some embodiments, AAH 2 has a SASA of at least about 200 Å 2 , at least about 210 Å 2 , at least about 220 Å 2 , at least about 240 Å 2 , at least about 250 Å 2 , at least about 260 Å 2 , at least about 270 Å 2 , at least about 280 Å 2 , at least about 290 Å 2 , at least about 300 Å 2 and at least about 310 Å 2 and at least about 320 Å 2 or at least about 330 Å 2 side chains. In some embodiments, AAH 1 and AAH 2 side chains have at least about 350 Å 2 and at least about 360 Å 2 and at least about 370 Å 2 and at least about 380 Å 2 and at least about 390 Å 2 and at least about 400 Å 2 and at least about 410 Å 2 and at least about 420 Å 2 and at least about 430 Å 2 and at least about 440 Å 2 and at least about 450 Å 2 and at least about 460 Å 2 and at least about 470 Å 2 and at least about 480 Å 2 and at least about 490 Å 2 and greater than about 500 Å 2 and at least about 510 Å 2 and at least about 520 Å 2 and at least about 530 Å 2 and at least about 540 Å 2 and at least about 550 Å 2, at least about 560 Å 2 , at least about 570 Å 2 , at least about 580 Å 2 , at least about 590 Å 2 , at least about 600 Å 2 , at least about 610 Å 2 , at least about 620 Å 2 , at least about 630 Å 2 , at least about 640 Å 2 , greater than about 650 Å 2 , at least about 660 Å 2 , at least about 670 Å 2 , at least about 680 Å 2 , at least about 690 Å 2 , or at least about 700 Å 2 of the combined SASA. In some embodiments, AA H2 is the SASA of the side chain is less than or equal to AA H1The SASA of the hydrophobic side chain of the hydrophobic amino acid. In some embodiments, the presence of a larger hydrophobic amino acid at the N-terminus and / or C-terminus of D-Arg or L-Arg in the CPP, or a combination thereof, improves the cytosolic delivery efficiency by about 1.1-fold to about 30-fold, such as about 1.2-fold, about 1.3-fold, about 1.4-fold, about 1.5-fold, about 1.6-fold, about 1.7-fold, about 1.8-fold, about 1.9-fold, about 2.0-fold, about 2.5-fold, about 3.0-fold, about 3.5-fold, about 4.0-fold, about 4.5-fold, about 5.0-fold, about 5.5-fold, about 6.0-fold, about 6.5-fold, about 7.0-fold, about 7.5-fold, about 8.0-fold, about 8.5-fold, about 9.0-fold, about 10-fold, about 10.5-fold, about 11.0-fold, about 11.5-fold, about 12.0-fold, about 12.5-fold, about 13.0-fold, about 13.5-fold, about 14.0-fold, about 14.5-fold, about 15.0-fold, about 15.5-fold, about 16.0-fold, about 16.5-fold, about 17.0-fold, about 17.5-fold, about 18.0-fold, about 18.5-fold, about 19.0-fold, about 19.5-fold, about 20-fold, about 20.5-fold, about 21.0-fold, about 21.5-fold, about 22.0-fold, about 22.5-fold, about 23.0-fold, about 23.5-fold, about 24.0-fold, about 24.5-fold, about 25.0-fold, about 25.5-fold, about 26.0-fold, about 26.5-fold, about 27.0-fold, about 27.5-fold, about 28.0-fold, about 28.5-fold, about 29.0-fold, or about 29.5-fold, including all values and subranges therebetween. In some embodiments, the CPP is at AA H2 -AA H1 -R-r, AA H2 -AA H1 -r-R, R-r-AA H1 -AA H2 、or r-R-AA H1 -AA H2 There are no hydrophobic amino acids at the N-terminus and / or C-terminus of. In a further embodiment, the CPP does not include a side chain larger than (as described herein) AA H1 or AA H2 Among the hydrophobic amino acids of at least one of. In a further embodiment, the CPP does not include a side chain with a surface area greater than AA H1hydrophobic amino acids. For example, in embodiments where at least one of AA H1 or AA H2 is phenylalanine, the CPP does not further include naphthylalanine (although the CPP includes at least one hydrophobic amino acid less than AA H1 and AA H2 such as leucine). In still other embodiments, the CPP, in addition to the hydrophobic amino acids in AA H2 -AA H1 -R-r, AA H2 -AA H1 -r-R, R-r-AA H1 -AA H2 , or r-R-AA H1 -AA H2 does not further include naphthylalanine. As discussed above, the chirality of the amino acids (i.e., D or L amino acids) can be selected to improve the cytosolic delivery efficiency of the CPP (and the attached cargo as described below). In some embodiments, the hydrophobic amino acid (e.g., AA H1 ) at the N-terminus or C-terminus of arginine has the same or opposite chirality as the adjacent arginine. In some embodiments, AA H1 has the opposite chirality to the adjacent arginine. For example, when arginine is D-arg (i.e., "r"), AA H1 is D-AA H1 , and when arginine is L-Arg (i.e., "R"), AA H1 is L-AA H1 . Thus, in some embodiments, the CPPs disclosed herein can include at least one of the following motifs: D-AA H1 -D-arg, D-arg-D-AA H1 , L-AA H1-L-Arg, or L-Arg-LAA H1 。In a specific embodiment, when the arginine is D-arg, AA H1 can be D-pip, D-nal, D-trp, D-bta, or D-phe. In another non-limiting example, when the arginine is L-Arg, AA H1 can be L-Pip, L-Nal, L-Trp, L-Bta, or L-Phe. In some embodiments, the presence of a hydrophobic amino acid having the same chirality as the adjacent arginine improves cytosolic delivery efficiency by about 1.1-fold to about 30-fold, such as about 1.2-fold, about 1.3-fold, about 1.4-fold, about 1.5-fold, about 1.6-fold, about 1.7-fold, about 1.8-fold, about 1.9-fold, about 2.0-fold, about 2.5-fold, about 3.0-fold, about 3.5-fold, about 4.0-fold, about 4.5-fold, about 5.0-fold, about 5.5-fold, about 6.0-fold, about 6.5-fold, about 7.0-fold, about 7.5-fold, about 8.0-fold, about 8.5-fold, about 9.0-fold, about 10-fold, about 10.5-fold, about 11.0-fold, about 11.5-fold, about 12.0-fold, about 12.5-fold, about 13.0-fold, about 13.5-fold, about 14.0-fold, about 14.5-fold, about 15.0-fold, about 15.5-fold, about 16.0-fold, about 16.5-fold, about 17.0-fold, about 17.5-fold, about 18.0-fold, about 18.5-fold, about 19.0-fold, about 19.5-fold, about 20-fold, about 20.5-fold, about 21.0-fold, about 21.5-fold, about 22.0-fold, about 22.5-fold, about 23.0-fold, about 23.5-fold, about 24.0-fold, about 24.5-fold, about 25.0-fold, about 25.5-fold, about 26.0-fold, about 26.5-fold, about 27.0-fold, about 27.5-fold, about 28.0-fold, about 28.5-fold, about 29.0-fold, or about 29.5-fold, including all values and subranges therebetween. In some embodiments, the CPPs described herein (e.g., CPPs according to Formulas IV-A to IV-P) include three arginines. Thus, in some embodiments, the CPPs described herein include one of the following sequences: AA H2 -AA H1 -R-r-R, AA H2 -AA H1 -R-r-r, AA H2 -AA H1-r-R-R, AA H2 -AA H1 -r-R-r, R-R-r-AA H1 -AA H2 , r-R-r-AA H1 -AA H2 , r-r-R-AA H1 -AA H2 , or R-r-R-AA H1 -AA H2 . In a specific embodiment, the CPP described herein has one of the following sequences: AA H2 -LAA H1 -R-r-R, AA H2 -DAA H1 -r-R-r, r-R-r-DAA H1 -AA H2 , or R-r-R-LAA H1 -AA H2 . In some embodiments, AAH 1 and AAH 2 chirality can be selected as described above, for example, to improve cytoplasmic uptake efficiency, where AAH 1 has the same chirality as the adjacent arginine, and AAH 1 and AAH 2 have opposite chirality. In some embodiments, the CPPs described herein (e.g., CPPs according to Formulas IV-A to IV-P) include three hydrophobic amino acids. Thus, in some embodiments, the CPPs described herein include one of the following sequences: AA H3 -AA H2 -AA H1 -Rr, AA H3 -AA H2 -AA H1 -Rr, AA H3 -AA H2 -AA H1 -rR、AA H3 -AA H2 -AA H1 -rR、Rr-AA H1 -AA H2 -AA H3 、Rr-AA H1 -AA H2 -AA H3 、rR-AA H1 -AA H2 -AA H3 , or rR-AA H1 -AA H2 -AA H3 , where AA H3 is any of the hydrophobic amino acids described above, such as piperidine-2-carboxylate, naphthylalanine, tryptophan, 3-(3-benzothienyl)-alanine, or phenylalanine. H1 AA H2 , and AA H3 The chirality of AAH can be selected, for example, as described above, to improve cytosol uptake efficiency, wherein 1has the same chirality as the adjacent arginine, and AA H1 and AA H2 have opposite chirality. In other embodiments, AA H1 、AA H2 、and AA H3 size can be selected as described above, for example, to improve cytoplasmic uptake efficiency, where AA H3 has a size less than or equal to AA H1 and separately / or AA H2 of the SAS. In some embodiments, AA H1 and AA H2 have the same or opposite chirality. In certain embodiments, AA H1 and AA H2 have opposite chirality. Thus, in some embodiments, the CPPs disclosed herein include at least one of the following sequences: D-AA H2 -L-AA H1 -R-r; L-AA H2 -D-AA H1 -r-R; R-r-D-AA H1 -L-AA H2 ; or r-R-L-AA H1 -D-AA H1 ,where each of D-AA H1 and D-AA H2 is a hydrophobic amino acid having the D configuration, and each of L-AA H1 and L-AA H2 is a hydrophobic amino acid having the L configuration. In some embodiments, D-AA H1 and D-AA H2 each of which is independently selected from the group consisting of D-pip, D-nal, D-trp, D-bta, and D-phe. In a specific embodiment, D-AA H1 or D-AA H2 is D-nal. In other specific embodiments, D-AA H1 is D-nal. In some embodiments, L-AA H1 and L-AA H2 each of which is independently selected from the group consisting of L-Pip, L-Nal, L-Trp, L-Bta, and L-Phe. In a specific embodiment, L-AA H1 or L-AA H2 is L-Nal. In other specific embodiments, L-AA H1 is L-Nal. In some embodiments, AA H1 and AA H2The presence improves cytoplasmic delivery efficiency by about 1.1-fold to about 30-fold, such as about 1.2-fold, about 1.3-fold, about 1.4-fold, about 1.5-fold, about 1.6-fold, about 1.7-fold, about 1.8-fold, about 1.9-fold, about 2.0-fold, about 2.5-fold, about 3.0-fold, about 3.5-fold, about 4.0-fold, about 4.5-fold, about 5.0-fold, about 5.5-fold, about 6.0-fold, about 6.5-fold, about 7.0-fold, about 7.5-fold, about 8.0-fold, about 8.5-fold, about 9.0-fold, about 10-fold, about 10.5-fold, about 11.0-fold, about 11.5-fold, about 12.0-fold, about 12.5-fold, about 13.0-fold, about 13.5-fold, about 14.0-fold, about 14.5-fold, about 15.0-fold, about 15.5-fold, about 16.0-fold, about 16.5-fold, about 17.0-fold, about 17.5-fold, about 18.0-fold, about 18.5-fold, about 19.0-fold, about 19.5-fold, about 20-fold, about 20.5-fold, about 21.0-fold, about 21.5-fold, about 22.0-fold, about 22.5-fold, about 23.0-fold, about 23.5-fold, about 24.0-fold, about 24.5-fold, about 25.0-fold, about 25.5-fold, about 26.0-fold, about 26.5-fold, about 27.0-fold, about 27.5-fold, about 28.0-fold, about 28.5-fold, about 29.0-fold, or about 29.5-fold, including all values and sub-ranges therebetween. Cargo portion The cargo portion can include any cargo of interest, such as a linker portion, a detectable portion, a therapeutic portion, a targeting portion, and the like, or any combination thereof. In some instances, the cargo portion can include one or more additional amino acids (such as K, UK, TRV); a linker (such as the bifunctional linker LC-SMCC); coenzyme A; phosphocoumaryl aminopropionic acid (pCAP); 8-amino-3,6-dioxaoctanoic acid (miniPEG); L-2,3-diaminopropionic acid (Dap or J); L-β-naphthylalanine; L-2-piperidinecarboxylic acid (Pip); sarcosine; benzene-1,3,5-tricarboxylic acid; 7-amino-4-methylcoumarin (Amc); fluorescein isothiocyanate (FITC); L-2-naphthylalanine; norleucine; 2-aminobutyric acid; rose bengal (Rho); dexamethasone (DEX); or a combination thereof. In some instances, the cargo portion can include any of those listed in Table 5, or derivatives or combinations thereof. Table 5 . Examples of cargo portion * pCAP, phosphocoumaryl aminopropionic acid; Ω, norleucine; U, 2-aminobutyric acid; D-pThr is D-phosphothreonine, and Pip is L-piperidine-2-carboxylate. Detectable portion The detectable moiety can include any detectable label. Examples of suitable detectable labels include, but are not limited to, UV-Vis labels, near-infrared labels, luminescent groups, phosphorescent groups, magnetic spin resonance labels, photosensitizers, photocleavable moieties, chelation centers, heavy atoms, radioisotopes, isotope-detectable spin resonance labels, paramagnetic moieties, chromophores, or any combination thereof. In some embodiments, the label can be detected without the addition of further reagents. In some embodiments, the detectable moiety is a biocompatible detectable moiety such that the compound is suitable for a variety of biological applications. As used herein, "biocompatible (biocompatible and biologically compatible)" generally refers to a compound, along with any metabolites or degradation products thereof, that is generally non-toxic to cells and tissues and does not cause any significant adverse effects on cells and tissues when the cells and tissues are incubated (e.g., cultured) in their presence. The detectable moiety can contain a luminescent group such as a fluorescent label or a near-infrared label. Examples of suitable luminescent groups include, but are not limited to, metal porphyrins; benzoporphyrins; azabenzoporphyrins; naphthoporphyrins; phthalocyanines; polycyclic aromatic hydrocarbons such as perylene, perylene diimide, pyrene; azo dyes; dyes; boron dipyrromethene, azaboron dipyrromethene, cyanine dyes, metal-ligand complexes such as ruthenium and iridium bipyridines, bipyridyls, phenanthrolines, coumarins, and acetylacetonates; acridine, derivatives such as benzoacridine ; azapentalene, squaric acid; 8-hydroxyquinoline, polymethine, luminescent nanoparticles such as quantum dots, nanocrystals; 2-hydroxyquinoline; terbium complexes; inorganic phosphors; ionophores such as crown ethers attached or derivatized with dyes; or combinations thereof. Specific examples of suitable luminescent groups include, but are not limited to, Pd(II) octaethylporphyrin; Pt(II)-octaethylporphyrin; Pd(II) tetraphenylporphyrin; Pt(II) tetraphenylporphyrin; Pd(II) meso-tetraphenylporphyrin tetrabenzoporphine; Pt(II) meso-tetraphenylmethylbenzoporphyrin; Pd(II) octaethylporphyrinone; Pt(II) octaethylporphyrinone; Pd(II) meso-tetra(pentafluorophenyl)porphyrin; Pt(II) meso-tetra(pentafluorophenyl)porphyrin; Ru(II) tris(4,7-diphenyl-1,10-phenanthroline) (Ru(dpp) 3 ) ; Ru(II) tris(1,10-phenanthroline) (Ru(phen) 3 )、tris(2,2'-bipyridine)ruthenium(II) hexahydrate (Ru(bpy) 3);Erythrosin B; Fluorescein; Fluorescein isothiocyanate (FITC); Eosin; Iridium(III) ((N-methyl-benzoimidazol-2-yl)-7-(diethylamino)-coumarin)); Indium(III) ((benzothiazol-2-yl)-7-(diethylamino)-coumarin)-2-(acetylacetonate); Lumogen dyes; Macroflex Fluorescent Red; Macrolex Fluorescent Yellow; Texas Red; Rhodamine B; Rhodamine 6G; Thiorhodamine; m-Cresol; Resorcinol Blue; Chrysophenol Blue; Cresol Red; Chlorophenol Blue; Bromocresol Green; Bromocresol Red; Bromothymol Blue; Cy2; Cy3; Cy5; Cy5.5; Cy7; 4-Nitrophenol; Alizarin; Phenolphthalein; o-Cresolphthalein; Chlorophenol Red; Calmagite; Bromo-chrysophenol; Phenol Red; Neutral Red; Nitrazine Yellow; 3,4,5,6-Tetrabromophenolphthalein; Congo Red; Fluorescein; Eosin; 2',7'-Dichlorofluorescein; 5(6)-Carboxy-fluorescein; Carboxynaphthofluorescein; 8-Hydroxypyrene-1,3,6-trisulfonic acid; Semi-naphthorhodafluor; Semi-naphthofluorescein; Tris(4,7-diphenyl-1,10-phenanthroline) ruthenium(II) dichloride; (4,7-Diphenyl-1,10-phenanthroline) ruthenium(II) tetraphenylborate; Platinum(II) octaethylporphyrin; Dialkylcarbocyanine; Dioctadecyl oxacarbocyanine; Fluorenylmethyloxycarbonyl chloride; 7-Amino-4-methylcoumarin (Amc); Green Fluorescent Protein (GFP); and derivatives or combinations thereof. In some examples, the detectable moiety may comprise Rhodamine B (Rho), Fluorescein isothiocyanate (FITC), 7-Amino-4-methylcoumarin (Amc), Green Fluorescent Protein (GFP), or derivatives or combinations thereof. The detectable moiety may be attached to the cell-penetrating peptide moiety at the amino, carboxylate group, or side chain of any amino acid in the cell-penetrating peptide moiety (e.g., at the amino, carboxylate group, or side chain of any amino acid in the CPP). Therapeutic moiety The disclosed compounds may also comprise a therapeutic moiety. In some examples, the cargo moiety comprises a therapeutic moiety. The detectable moiety may be linked to the therapeutic moiety or the detectable moiety may also serve as the therapeutic moiety. A therapeutic moiety refers to a moiety that when administered to a subject will reduce one or more symptoms of a disease or disorder. The therapeutic moiety may comprise a variety of drugs, including antagonists such as enzyme inhibitors, and agonists such as transcription factors that result in increased expression of a desired gene product (although antagonistic transcription factors may also be used as would be understood by one of ordinary skill in the art). In addition, the therapeutic moiety includes those agents that are capable of directing toxicity and / or capable of inducing toxicity to healthy and / or unhealthy cells in the body. In addition, the therapeutic moiety may be capable of inducing and / or triggering the immune system against potential pathogens. The treatment part may for example include an anticancer agent, an antiviral agent, an antimicrobial agent, an anti-inflammatory agent, an immunosuppressive agent, an anesthetic agent, or any combination thereof. The treatment portion may include anti-cancer agents. Examples of anti-cancer agents include 13-cis-retinoic acid, 2-amino-6-mercaptopurine, 2-CdA, 2-chlorodeoxyadenosine, 5-fluorouracil, 6-thioguanine, 6-mercaptopurine, Accutane, actinomycin-D, doxorubicin, Adrucil, Agrylin, Ala-Cort, aldesleukin, alemtuzumab, acitretin, Alkaban-AQ, Alkeran, all-trans-retinoic acid, alpha interferon, hexamethylmelamine, methotrexate, amifostine, aminoglutethimide, anagrelide, Anandron, anastrozole, cytarabine, Aranesp, Aredia, Arimidex, Aromasin, arsenic trioxide, asparaginase, ATRA, Avastin, BCG, BCNU, bevacizumab, bexarotene, bicalutamide, BiCNU, Blenoxane, bleomycin, bortezomib, busulfan, Busulfex, C225, calcium folinate, Campath, Camptosar, irinotecan, capecitabine, Carac, carboplatin, carmustine, carmustine wafer, Casodex, CCNU, CDDP, CeeNU, Cerubidine, cetuximab, chlorambucil, cisplatin, citrovorum factor, cladribine, cortisone, Cosmegen, CPT-11, cyclophosphamide, Cytadren, cytarabine, liposomal cytarabine, Cytosar-U, Cytoxan, dacarbazine, actinomycin D, Darbepoetin alfa, daunomycin, daunorubicin, daunorubicin hydrochloride, liposomal daunorubicin, DaunoXome, Decadron, δ-Cortef, Deltasone, denileukin-diftitox, DepoCyt, dexamethasone, dexamethasone acetate, dexamethasone sodium phosphate, Dexasone, dexrazoxane, DHAD, DIC, Diodex, docetaxel, Doxil, doxorubicin, liposomal doxorubicin, Droxia, DTIC, DTIC-Dome, Duramycin, Efudex, Eligard, Elspar, Oxaliplatin, espar, Emcyt, epirubicin, epoetin alfa, Erbitux, Erwinia L-asparaginase, estramustine, Ethyol, Famvir, etoposide, etoposide phosphate, Eulexin, Evista, exemestane, Fareston, Fludara, fludarabine, Fluoroplex, fluorouracil, fluorouracil (cream), fluoxymesterone, flutamide, folinic acid, FUDR, fulvestrant, G-CSF, gefitinib, gemcitabine, gemtuzumab ozogamicin, Gemzar, Gleevec, Lupron, LupronDepot, Matulane, Maxidex, methyl bis(2-chloroethyl)amine, methyl bis(2-chloroethyl)amine hydrochloride, Medrol, Medrol, Megace, megestrol acetate, melphalan, mercaptopurine, mesna, Mesnex, methotrexate, methotrexate sodium, methylprednisolone, Mylocel, letrozole, Neosar, Neulasta, Nimotuzumab, Youbaojin, nilutamide, nilutamide, nitrogen mustard, Novaldex, Novantrone, octreotide, octreotide acetate, Oncospar, vincristine, Ontak, Onxal, Oprelvekin, Orapred, Orasone, oxaliplatin, paclitaxel, pamidronate, Panretin, Paraplatin, Pediapred, PEG interferon, pegaspargase, pegfilgrastim, PEG-INTRON, PEG-L-asparaginase, phenylalanine mustard, Platinol, Platinol-AQ, prednisone, prednisone, Prelone, procarbazine, PROCRIT, Purizen, Proflavine 20 with carmustine implant, Purinethol, raloxifene, Rheumatrex, Rituxan, rituximab, Roveron-A (interferon α-2a), Rubex, rubidomycin hydrochloride, Sandostatin, Sandostatin LAR, sargramostim, Solu-Cortef, Solu-Medrol, STI-571, streptozocin, tamoxifen, targretin, paclitaxel, Kelaie, Temodar, temozolomide, teniposide, TESPA, thalidomide, thalidomide, TheraCys, thioguanine, thioguanine tablets, thiotepa, Thioplex, thiotepa, TICE, Toposar, topotecan, toremifene, trastuzumab, tretinoin, Trexall, Trisenox, TSPA, VCR, Velban, Velcade, VePesid, Vesanoid, Viadur, vinblastine, vinblastine sulfate, Vincasar Pfs, vincristine, vinorelbine, vinorelbine tartrate, VLB, VP-16,威猛, Jieliu Da, Zanosar, Zevalin, Zinecard, Zoladex, zoledronic acid, Zometa, Gliadel wafers, Glivec, GM-CSF, goserelin, granulocyte colony-stimulating factor, fluoxymesterone, Herceptin, Hexadrol, Hexalen, hexamethylmelamine, HMM, Aikangding, Aizhi, hydrocortisone acetate, hydrocortisone, hydrocortisone sodium phosphate, hydrocortisone sodium succinate, hydrocortisone phosphate, hydroxyurea, Ibritumomab,替伊莫单抗, idarubicin, idarubicin, Ifex, IFN-α, Ifosfamide, IL2. IL-11, imatinib mesylate, imidazole carboxamide, interferon α, interferon α-2b (PEG conjugate), interleukin 2, interleukin-11, Intron A (interferon α-2b), folinic acid, busulfan, Leukine, leuprorelin, vincristine, vinblastine, liposomal Ara-C, liquid Pred, lomustine, L-PAM, L-sarcolysin, Meticorten, mitomycin, mitomycin-C, mitoxantrone, M-prednisone, MTC, MTX, Mustargen, nitrogen mustard, mutamycin, Myleran, Iressa, irinotecan, isotretinoin, Kidrolase, Lanacort, L-asparaginase, and LCR. The treatment portion may also include biological agents such as, for example, antibodies. In some instances, the treatment portion may include antiviral agents such as ganciclovir, azidothymidine (AZT), lamivudine (3TC), and the like. In some instances, the therapeutic portion may include antibacterial agents such as dapsone; sodium acetylsulfadiazine; alethromycin; alexidine; mecillinam; pivmecillinam; amicycline; amifloxacin; amifloxacin mesylate; amikacin; amikacin sulfate; aminosalicylic acid; sodium aminosalicylate; amoxicillin; amphotericin; ampicillin; sodium ampicillin; apalcillin sodium; apramycin; apramycin; asomamycin sulfate; avilamycin; avoparcin; azithromycin; azlocillin; azlocillin sodium; bacampicillin hydrochloride; bacitracin; bacitracin methylene disalicylate; bacitracin zinc; bambuterol; calcium benzoate; erythromycin B; betamethasone sulfate; biapenem; biniramycin; phenyl salicylate hydrochloride; pyrantel pamoate magnesium sulfate; butikacin; butirosin sulfate; viomycin sulfate; carbadox; carbenicillin disodium; carbenicillin indanyl sodium; carbenicillin phenyl sodium; carbenicillin potassium; carumonam sodium; cefaclor; cefazedone; cefamandole; cefamandole nafate; cefamandole sodium; cefaparole; cefatrizine; cefazolin sodium; cefroxadine; cefroxadine sodium; cefbuperazone; cefdinir; cefepime; cefepime hydrochloride; cefotiam; cefotiam hydrochloride; cefmetazole; cefmetazole sodium; cefonicid monosodium; cefonicid sodium; cefoperazone sodium; ceforanide; cefotaxime sodium; cefotetan; cefotetan disodium; cefotiam hydrochloride; cefoxitin; cefoxitin sodium; cefpimizole; cefpimizole sodium; cefpiramide; cefpiramide sodium; cefpirome sulfate; cefpodoxime proxetil; cefprozil; cefroxadine; cefradine sodium; cefotaxime; cefibuten; cefotaxime sodium; ceftriaxone sodium; cefuroxime; cefuroxime axetil; cefuroxime pivoxetil; cefuroxime sodium; cefacetrile sodium; cefalexin; cefalexin hydrochloride; cefaloglycin; cephaloridine; cephalothin sodium; cefapirin sodium; cefroxadine; cefaclor hydrochloride; chloramphenicol; chloramphenicol; chloramphenicol palmitate; chloramphenicol pantothenate complex; chloramphenicol sodium succinate; chlorhexidine aminobenzenephosphate; chloroxylenol; chlortetracycline bisulfate; chlortetracycline hydrochloride; cinoxacin; ciprofloxacin; ciprofloxacin hydrochloride; cirotomycin; clarithromycin; clinafloxacin hydrochloride; clindamycin; clindamycin hydrochloride; clindamycin palmitate hydrochloride; clindamycin phosphate; clofazimine; benzathine cloxacillin; cloxacillin sodium; chloroquine; colistin methanesulfonate; colistin sulfate; coumermycin; coumermycin sodium; cyclacillin; cycloserine; dalfopristin; dapsone; daptomycin; demeclocycline; demeclocycline hydrochloride; desmethylchlortetracycline; diniconazole; diaminopyridine; dicloxacillin; dicloxacillin sodium; streptomycin sulfate; dipyrithione; dirithromycin; doxycycline; doxycycline calcium; doxycycline phosphate complex; doxycycline hydrochloride; droxacin sodium; enoxacin; epicillin; epitetracycline hydrochloride; erythromycin; erythromycin estolate; erythromycin ethylsuccinate; erythromycin gluceptate; erythromycin lactobionate; erythromycin propionate;Erythromycin stearate; Ethambutol hydrochloride; Ethionamide; Fleroxacin; Flucloxacillin; Fluorodalanine; Flumequine; Fosfomycin; Fosfomycin trometamol; Fumoxicillin; Furazochloride; Fursultiamine tartrate; Fusidic acid sodium; Fusidic acid; Sulfocidin sulfate; Glomoxan; Bacitracin; Haloprogin; Hetacillin; Hetacillin potassium; Hexetidine; Ibafloxacin; Imipenem; Isoconazole; Isepamicin; Isonicotinic acid tincture; Josamycin; Kanamycin sulfate; Kitasamycin; Levofuraltadone; Levopipicillin potassium; Lymecycline; Lincomycin; Lincomycin hydrochloride; Lomefloxacin; Lomefloxacin hydrochloride; Lomefloxacin mesylate; Cefaclor; Mafenide; Methacycline; Methacycline sulfosalicylate; Megamycin potassium phosphate; Mequindox; Meropenem; Metacycline; Metacycline hydrochloride; Hexamethylenetetramine; Hexamethylenetetramine hippurate; Hexamethylenetetramine mandelate; Methicillin sodium; Metiprim; Metronidazole hydrochloride; Metronidazole phosphate; Mezlocillin; Mezlocillin sodium; Minocycline; Minocycline hydrochloride; Milimycin hydrochloride; Monensin; Monensin sodium; Nafcillin sodium; Nalidixic acid sodium; Nalidixic acid; Natamycin; Nilmicin; Neomycin palmitate; Neomycin sulfate; Neomycin undecylenate; Netilmicin sulfate; Neutramycin; Nitrofurazene; Nitrofurazone; Nitrofurantoin; Nitrofuridazone; Nitrofuradiazole; Nitrofurmit; Nitrofurpyridol; Nitrofurquazone; Nitrofurthiazole; Nitrocycline; Nitrofurantoin; Nitromid; Norfloxacin; Novobiocin sodium; Ofloxacin; Onartoprim; Oxacillin; Oxacillin sodium; Omoroxan; Omoroxan sodium; Oxolinic acid; Oxytetracycline; Oxytetracycline calcium; Oxytetracycline hydrochloride; Pardomycin; p-Chlorophenol; Paulomycin; Pefloxacin; Pefloxacin mesylate; Penicillinase-resistant penicillin; Benzathine penicillin G; Penicillin G potassium; Procaine penicillin G; Penicillin G sodium; Penicillin V; Benzathine penicillin V; Phenoxymethylpenicillin V; Penicillin V potassium; Pentizidone sodium; Phenylaminosalicylate; Piperacillin sodium; Picobenzylpenicillin sodium; Pivampicillin sodium; Pyridomycin hydrochloride; Pivampicillin hydrochloride; Pivampicillin embonate; Pivampicillin propionate; Polymyxin B sulfate; Porfiromycin; Piptazocin; Pyrazinamide; Zinc pyrithione; Quindecamine acetate; Quinupristin; Racemethionine sulfoxide; Ramoplanin; Renimycin; Relomycin; Riparicin; Rifabutin; Rifametane; Rifaxidine; Rifamide; Rifapentine; Rifaximin; Rolitetracycline; Rolitetracycline nitrate; Rosaramicin; Rosaramicin butyrate; Rosaramicin propionate; Rosaramicin sodium phosphate; Rosaramicin stearate; Roxoxacin; Roxarsone; Roxithromycin; Sancycline; Sefepime sodium; Samoxicillin; Sarpicillin; Sisomicin; Sisomicin sulfate; Sparfloxacin; Spectinomycin hydrochloride; Spiramycin; Stathomycin hydrochloride; Stetomycin; Streptomycin sulfate; Streptomycin nicotinate; Sulfabenz; Sulfanilamide; Acetylsulfanilamide; Acetylsulfanilamide sodium; Sulfacetamide; Sulfadiazine; Sulfadiazine sodium; Sulfadoxine;Sulphalin; Sulfamethazine; Sulfamethoxydiazine; Sulfamethazine; Sulfamethizole; Sulfamethoxazole; Sulfamonomethoxine; Sulfisoxazole; Zinc Sulfanilate; Sulfanitran; Sulfasalazine; Sulfisotiazole; Sulfathiazole; Sulfapyrazole; Sulfaisomer; isoxazole; Sulfaisomer isoxazole acetyl; Sulfaisomer isoxazole diethanolamine; Sulfacolistin; Thienamycin; Sultamicillin; Cloxacillin Sodium; Talampicillin Hydrochloride; Teicoplanin; Temafloxacin Hydrochloride; Temocillin; Tetracycline; Tetracycline Hydrochloride; Tetracycline Phosphate Complex; Trimethoprim; Thiamphenicol; Ticarcillin Potassium; Ticarcillin Toluene Sulfonate; Ticarcillin Disodium; Ticarcillin Monosodium; Ticlatone; Chlorobenzene Thiodine Chloride; Tobramycin; Tobramycin Sulfate; Trovafloxacin; Trimethoprim; Trimethoprim Sulfate; Trisulfapyrimidines; Oleandomycin; Propionylspiramycin Sulfate; Brevibacterin; Vancomycin; Vancomycin Hydrochloride; Virginiamycin; or Ramoplanin. In some examples, the therapeutic portion may include an anti-inflammatory agent. In some examples, the therapeutic portion may include dexamethasone (Dex). In other examples, the therapeutic portion includes a therapeutic protein. For example, some people have certain enzyme deficiencies (such as lysosomal storage diseases). Disclosed herein is the delivery of such enzymes / proteins to human cells by linking the enzyme / protein to one of the disclosed cell-penetrating peptides. The disclosed cell-penetrating peptides have been tested with proteins (such as GFP, PTP1B, actin, calmodulin, troponin C) and shown to be functional. In some examples, the therapeutic portion includes a targeting portion. The targeting portion may include, for example, an amino acid sequence that can target one or more enzyme domains. In some examples, the targeting portion may include an inhibitor against an enzyme that can act in diseases such as cancer, cystic fibrosis, diabetes, obesity, or a combination thereof. For example, the targeting portion may include any of the sequences listed in Table 6. Table 6. Examples of targeting portions * Fpa, Σ: L-4-fluorophenylalanine; Pip, Θ: L-proline; Nle, Ω: L-norleucine; Phg, Ψ L-phenylglycine; F 2 Pmp, Λ: L-4-(phosphonyldifluoromethyl)phenylalanine; Dap, L-2,3-diaminopropionic acid; Nal, Φ’: L-β-naphthylalanine; Pp, ϑ: L-pipecolic acid; Sar, Ξ: sarcosine; Tm, benzene-1,3,5-tricarboxylic acid. The targeting portion and the cell-penetrating peptide portion may overlap. That is, the residues that form the cell-penetrating peptide portion may also be part of the sequence that forms the targeting portion, and vice versa. The therapeutic moiety can be attached to the cell-penetrating peptide moiety at the amino group, carboxylate group, or side chain of any amino acid in the cell-penetrating peptide moiety (e.g., at the amino group, carboxylate group, or side chain of any amino acid in the CPP). In some examples, the therapeutic moiety can be attached to a detectable moiety. In some examples, the therapeutic moiety can include a targeting moiety that can act as an inhibitor against Ras (e.g., K-Ras), PTP1B, Pin1, Grb2 SH2, CAL PDZ, and the like, or a combination thereof. Ras is a protein encoded by the RAS gene in humans. Normal Ras protein performs essential functions in normal tissue signaling, and mutations in the Ras gene are known to be involved in the development of many cancers. Ras can act as a switch of a molecular on / off switch, and once turned on, Ras attracts and activates the proteins required to transmit growth factor and other receptor signals. Mutant forms of Ras are known to be involved in various cancers, including lung cancer, colon cancer, pancreatic cancer, and various leukemias. Protein-tyrosine phosphatase 1B (PTP1B) is a prototype member of the PTP superfamily and has many roles during eukaryotic cell signaling. PTP1B is a negative regulator of the insulin signaling pathway and is regarded as a promising potential therapeutic target, especially for the treatment of type II diabetes. PIP1B is also known to be involved in the development of breast cancer. Pin1 is an enzyme that binds to a subset of proteins and plays a role in post-phosphorylation control in regulating protein function. Pin1 activity can regulate the outcome of proline-directed kinase signaling and thus can regulate cell proliferation and cell survival. Downregulation of Pin1 can have an effect in various diseases. Upregulation of Pin1 may be involved in certain cancers, and downregulation of Pin1 may be involved in Alzheimer's disease. Pin1 inhibitors can have therapeutic effects on cancers and immune disorders. Grb2 is an adaptor protein involved in signal transduction and cell communication. The Grb2 protein contains an SH2 domain that can bind tyrosine phosphorylation sequences. Grb2 is widely expressed and is essential for a variety of cellular functions. Inhibiting Grb2 function can impair developmental processes and can block the transformation and proliferation of various cell types. Recently, it has been reported that the activity of cystic fibrosis transmembrane conductance regulator (CFTR), a chloride channel protein mutated in patients with cystic fibrosis (CF), is negatively regulated by CFTR-related ligand (CAL) via its PDZ domain (CAL-PDZ) (Wolde, M et al J. Biol.Chem.2007, 282, 8099). Inhibiting the CFTR / CAL-PDZ interaction has been shown to improve the activity of the most common CFTR mutant form, ∆Phe508-CFTR (Cheng, SH et al Cell1990, 63, 827; Kerem, BS et al. Science1989, 245, 1073), which is achieved by reducing its proteasome-mediated degradation (Cushing, PR et al. Angew.Chem.Int. Ed.2010, 49, 9907). Accordingly, a method of treating a subject having cystic fibrosis by administering an effective amount of a compound or composition disclosed herein is disclosed herein. The compound or composition administered to the subject may comprise a therapeutic moiety, which may comprise a targeting moiety that can act as an inhibitor against CAL PDZ. Additionally, the compound or composition disclosed herein may be administered in combination with a molecule that corrects CFTR function. A composition comprising a compound described herein is also disclosed herein. The pharmaceutically acceptable salts and prodrugs of the disclosed compounds are also disclosed herein. Pharmaceutically acceptable salts include salts of the disclosed compounds prepared with an acid or a base depending on the specific substituents found on the compound. Under conditions where the compounds disclosed herein are sufficiently basic or acidic to form stable, non-toxic acid or base salts, it may be appropriate to administer the compounds in the form of salts. Examples of pharmaceutically acceptable base addition salts include sodium, potassium, calcium, ammonium, or magnesium salts. Examples of physiologically acceptable acid addition salts include hydrochloric acid, hydrobromic acid, nitric acid, phosphoric acid, carbonic acid, sulfuric acid, and organic acids such as acetic acid, propionic acid, benzoic acid, succinic acid, fumaric acid, mandelic acid, oxalic acid, citric acid, tartaric acid, malonic acid, ascorbic acid, α-ketoglutaric acid, α-glycerophosphate, maleic acid, toluenesulfonic acid, methanesulfonic acid, and the like. Accordingly, what is disclosed herein are hydrochloride, nitrate, phosphate, carbonate, bicarbonate, sulfate, acetate, propionate, benzoate, succinate, fumarate, mandelate, oxalate, citrate, tartrate, malonate, ascorbate, α-ketoglutarate, α-glycerophosphate, maleate, toluenesulfonate, and methanesulfonate. Pharmaceutically acceptable salts of the compounds can be obtained using standard procedures well known in the art, for example, by reacting a sufficiently basic compound such as an amine with a suitable acid to provide a physiologically acceptable anion. Alkali metal (e.g., sodium, potassium, or lithium) or alkaline earth metal (e.g., calcium) salts of carboxylic acids can also be prepared. Manufacturing methods In some embodiments, the CPPs disclosed herein are prepared using a peptide according to any one of Formulas V-A to V-D: 、 、 、 or , wherein: AA H1 and AA H2 each of which is independently selected from hydrophobic amino acids; AA U and AA Z each occurrence is independently selected from amino acids, and each AA U and each AA Z at most one of which is arginine (i.e., provided that the cyclic peptide does not include more than 3 arginines); and each of m and n is a number from 0 to 6, provided that at least one of m or n is not 0. In some embodiments, methods of preparing the peptides disclosed herein include contacting a peptide (or any amino acid thereof) according to any one of Formulas V-A to V-D with a support (such as those described below). In some embodiments, the amino group at the N-terminus and the carboxylate group at the C-terminus of the peptide of Formula V-A, V-B, V-C, or V-D independently form a peptide bond. For example, in some embodiments, the N-terminus of the peptide can form a peptide bond with the C-terminus of the peptide, thereby forming a cyclic peptide. In alternative embodiments, the N-terminus and the C-terminus can independently form a peptide bond with the cyclizing moiety, thereby forming a cyclic peptide. In still other embodiments, covalent bonds can form between the side chains of the amino acids in the peptide of Formula V-A, V-B, V-C, or V-D, thereby forming a cyclic peptide. In some embodiments, the peptide further comprises a cyclizing moiety by which to form a cyclic peptide. The cyclizing moiety can be any moiety suitable for interacting with an amino acid of any one of Formulas V-A to V-D to thereby form a cyclic peptide. In some embodiments, the cyclizing moiety independently forms a peptide bond with the amino group at the N-terminus and the carboxylate group at the C-terminus of an amino acid at opposite ends of the peptide of any one of Formulas V-A to V-D. In embodiments, the cyclizing moiety can be a natural or non-natural amino acid. In some embodiments, one or more amino acids in the CPP can also be part of the cyclizing moiety. In some embodiments, the cyclizing moiety is glutamic acid. In some embodiments, the peptide further comprises a cargo moiety X n , wherein at least one atom or bond is attached to X n and the bond to X n comprises, for example, a therapeutic moiety, a targeting moiety, a detectable moiety, or a combination thereof as described above. In some embodiments, the amino acids in the CPP of Formulas V-A to V-D (including r, R, AA H1 , AA H2 ) The total number is in the range of 6 to 10. In some embodiments, the total number of amino acids is 6. In some embodiments, the total number of amino acids is 7. In some embodiments, the total number of amino acids is 8. In some embodiments, the total number of amino acids is 9. In some embodiments, the total number of amino acids is 10. In some embodiments, the sum of m and n is 2 to 6. In some embodiments, the sum of m and n is 2. In some embodiments, the sum of m and n is 3. In some embodiments, the sum of m and n is 4. In some embodiments, the sum of m and n is 5. In some embodiments, the sum of m and n is 6. In some embodiments, m is 0. In some embodiments, m is 1. In some embodiments, m is 2. In some embodiments, m is 3. In some embodiments, m is 4. In some embodiments, m is 5. In some embodiments, m is 6. In some embodiments, n is 0. In some embodiments, n is 1. In some embodiments, n is 2. In some embodiments, n is 3. In some embodiments, n is 4. In some embodiments, n is 5. In some embodiments, n is 6. As discussed above, the hydrophobicity of the amino acids in the CPPs disclosed herein can be selected to improve the uptake efficiency. In some embodiments, AA H1 and AA H2 each independently is a hydrophobic amino acid having a hydrophobicity value greater than that of glycine. In other embodiments, AA H1 and AA H2 each independently is a hydrophobic amino acid having a hydrophobicity value greater than that of alanine. In still other embodiments, AA H1 and AA H2Each of them is independently a hydrophobic amino acid having a hydrophobicity value greater than that of phenylalanine, as measured, for example, using the hydrophobicity scales described above, including Eisenberg and Weiss (Proc. Natl. Acad. Sci. U. S. A. 1984; 81(1):140–144), Engleman, et al. (Ann. Rev. of Biophys. Biophys. Chem.. 1986; 1986(15):321–53), Kyte and Doolittle (J. Mol. Biol. 1982; 157(1):105–132), Hoop and Woods (Proc. Natl. Acad. Sci. U. S. A. 1981; 78(6):3824–3828), and Janin (Nature. 1979; 277(5696):491–492) (see Table 1 above). In a specific embodiment, hydrophobicity is measured using the hydrophobicity scale reported by Engleman et al. As described above, it has also been found that the presence of hydrophobic amino acids at the N-terminus or C-terminus of D-Arg or L-Arg, or in combination thereof, improves the cytosolic uptake of CPP (and attached cargo). For example, in some embodiments, the CPPs disclosed herein may include AA H1 -D-Arg or D-Arg-AA H1 . In other embodiments, the CPPs disclosed herein may include AA H1 -L-Arg or L-Arg-AA H1 . As discussed above, hydrophobic amino acids at the N-terminus or C-terminus of D-Arg or L-Arg, or in combination thereof, can be selected (i.e., AA H1), to improve the cytoplasmic delivery efficiency of CPP. For example, a larger hydrophobic amino acid at the N-terminus or C-terminus of D-Arg or L-Arg, or a combination thereof, improves cytoplasmic delivery efficiency compared to a sequence otherwise identical with a smaller hydrophobic amino acid. As discussed above, the size of the hydrophobic amino acid can be measured in terms of the molecular weight of the hydrophobic amino acid, the steric effect of the hydrophobic amino acid, the solvent-accessible surface area (SASA) of the side chain, or a combination thereof. In some embodiments, the size of the hydrophobic amino acid is measured in terms of the molecular weight of the hydrophobic amino acid, and the larger hydrophobic amino acid has a side chain with a molecular weight of at least about 90 g / mol, or at least about 130 g / mol, or at least about 141 g / mol. In other embodiments, the size of the amino acid is measured in terms of the SASA of the hydrophobic side chain, and the larger hydrophobic amino acid has a side chain with a SASA greater than alanine, or greater than glycine. In other embodiments, AA H1 has a hydrophobic side chain with a SASA greater than or equal to about piperidine-2-carboxylate, greater than or equal to about tryptophan, greater than or equal to about phenylalanine, or equal to or greater than about naphthylalanine. In some embodiments, AA H1 and AA H2 independently have a side chain with a SASA in the range of about 200 Å 2 to about 1000 Å 2 For example, about 250 Å 2 、300 Å 2 、350 Å 2 、400 Å 2 、450 Å 2 、500 Å 2 、550 Å 2 、650 Å 2 、700 Å 2 、750 Å 2 、800 Å 2 、850 Å 2 、900 Å 2, and about 950 Å 2 , including all values and sub - ranges therebetween. In some embodiments, AA H1 has a SASA of at least about 200 Å 2 , at least about 210 Å 2 , at least about 220 Å 2 , at least about 240 Å 2 , at least about 250 Å 2 , at least about 260 Å 2 , at least about 270 Å 2 , at least about 280 Å 2 , at least about 290 Å 2 , at least about 300 Å 2 , at least about 310 Å 2 , at least about 320 Å 2 , or at least about 330 Å 2 of the side chain. In some embodiments, AAH 2 has a SASA of at least about 200 Å 2 , at least about 210 Å 2 , at least about 220 Å 2 , at least about 240 Å 2 , at least about 250 Å 2 , at least about 260 Å 2 , at least about 270 Å 2 , at least about 280 Å 2 , at least about 290 Å 2 , at least about 300 Å 2 , at least about 310 Å 2 , at least about 320 Å 2 , or at least about 330 Å 2 of the side chain. In some embodiments, AAH 1 and AAH 2 of the side chain have at least about 350 Å 2 , at least about 360 Å 2 , at least about 370 Å 2 , at least about 380 Å 2 , at least about 390 Å 2 , at least about 400 Å 2 , at least about 410 Å 2 , at least about 420 Å 2 , at least about 430 Å 2 , at least about 440 Å 2 , at least about 450 Å 2 , at least about 460 Å 2 , at least about 470 Å 2 , at least about 480 Å 2 , at least about 490 Å 2 , greater than about 500 Å 2 , at least about 510 Å 2 , at least about 520 Å 2 , at least about 530 Å 2 , at least about 540 Å 2 , at least about 550 Å 2 , at least about 560 Å 2 , at least about 570 Å 2 , at least about 580 Å 2 , at least about 590 Å 2 , at least about 600 Å 2 , at least about 610 Å 2 , at least about 620 Å 2 , at least about 630 Å 2 , at least about 640 Å 2 , greater than about 650 Å 2 , at least about 660 Å 2 , at least about 670 Å 2 , at least about 680 Å 2 , at least about 690 Å 2 , or at least about 700 Å 2 of the combined SASA. In some embodiments, AA H2 is a hydrophobic amino acid in which the SASA of the side chain is less than or equal to AA H1 of the SASA of the hydrophobic side chain. In some embodiments, CPP is in AA H2 -AA H1 -R-r, AA H2 -AA H1 -r-R, R-r-AA H1 -AA H2 , or r-R-AA H1 -AA H2 does not include hydrophobic amino acids at the N-terminus and / or C-terminus of. In alternative embodiments, CPP does not include a side chain greater than (as described herein) AA H1 or AA H2 hydrophobic amino acids of at least one of them. In a further embodiment, the CPP does not include a hydrophobic amino acid with a side chain surface area greater than AA H1 hydrophobic amino acid. For example, in AA H1 or AA H2 in an embodiment where at least one of them is phenylalanine, the CPP does not further include naphthylalanine (although the CPP includes at least one less than AA H1 and AA H2 hydrophobic amino acids, such as leucine). In still other embodiments, the CPP, in addition to in AA H2 -AA H1 -R-r, AA H2 -AA H1 -r-R, R-r-AA H1 -AA H2 、or r-R-AA H1 -AA H2 does not include naphthylalanine other than the hydrophobic amino acids in. As discussed above, the chirality of the amino acid can be selected (i.e., D or L amino acid) to improve the cytosolic delivery efficiency of the CPP (and the attached cargo as described below). In some embodiments, the hydrophobic amino acid (such as AA H1 ) at the N-terminus or C-terminus of arginine has the same or opposite chirality as the adjacent arginine. In some embodiments, AA H1 has the opposite chirality to the adjacent arginine. For example, when arginine is D-arg (i.e., "r"), AA H1 is D-AA H1 , and when arginine is L-Arg (i.e., "R"), AA H1 is L-AA H1 . Thus, in some embodiments, the CPPs disclosed herein may include at least one of the following motifs: D-AA H1 -D-arg, D-arg-D-AA H1 , L-AA H1 -L-Arg, or L-Arg-LAA H1 . In a specific embodiment, when the arginine is D-arg, AA H1 can be D-pip, D-nal, D-trp, D-bta, or D-phe. In another non-limiting example, when the arginine is L-Arg, AA H1 can be L-Pip, L-Nal, L-Trp, L-Bta, or L-Phe. In some embodiments, the CPPs described herein (e.g., CPPs according to Formulas V-A to V-D) include three arginines. Thus, in some embodiments, the CPPs described herein include one of the following sequences: AA H2 -AA H1 -R-r-R, AA H2 -AA H1 -R-r-r, AA H2 -AA H1 -r-R-R, AA H2 -AA H1 -r-R-r, R-R-r-AA H1 -AA H2 , r-R-r-AA H1 -AA H2 , r-r-R-AA H1 -AA H2 , or R-r-R-AA H1 -AA H2 . In a specific embodiment, the CPPs described herein have one of the following sequences: AA H2 -AA H1 -R-r-R, AA H2 -AA H1 -r-R-r, r-R-r-AA H1 -AA H2 or R-r-R-AA H1 -AA H2 。In some embodiments, AA H1 and AA H2 's chirality can be selected as described above to improve the cytoplasmic uptake efficiency, where AA H1 has the same chirality as the adjacent arginine, and AA H1 and AA H2 have opposite chirality. In some embodiments, the CPPs described herein (e.g., CPPs according to Formulas V-A to V-D) include three hydrophobic amino acids. Thus, in some embodiments, the CPPs described herein include one of the following sequences: AA H3 -AA H2 -AA H1 -R-r, AA H3 -AA H2 -AA H1 -R-r, AA H3 -AA H2 -AA H1 -r-R, AA H3 -AA H2 -AA H1 -r-R, R-r-AA H1 -AA H2 -AA H3 、R-r-AA H1 -AA H2 -AA H3 、r-R-AA H1 -AA H2 -AA H3 、 or r-R-AA H1 -AA H2 -AA H3 , wherein AA H3 is any of the above hydrophobic amino acids, such as piperidine-2-carboxylate, naphthylalanine, tryptophan, 3-(3-benzothienyl)-alanine, or phenylalanine. In some embodiments, AA H1 、AA H2 、 and AA H3 's chirality can be selected as described above to improve the cytoplasmic uptake efficiency, wherein AAH 1 has the same chirality as the adjacent arginine, and AA H1 and AA H2 have opposite chirality. In other embodiments, AA H1 、AA H2 、 and AA H3 's size can be selected as described above to improve the cytoplasmic uptake efficiency, wherein AA H3 has a size less than or equal to AA H1 and separately / or AA H2 's SAS. In some embodiments, AA H1 and AA H2Have the same or opposite chirality. In certain embodiments, AA H1 and AA H2 Have opposite chirality. Thus, in some embodiments, the CPPs disclosed herein include at least one of the following sequences: D-AA H2 -L-AA H1 -R-r; L-AA H2 -D-AA H1 -r-R; R-r-D-AA H1 -L-AA H2 ; or r-R-L-AA H1 -D-AA H1 , where each of D-AA H1 and D-AA H2 is a hydrophobic amino acid having a D configuration, and each of L-AA H1 and L-AA H2 is a hydrophobic amino acid having an L configuration. In some embodiments, each of D-AA H1 and D-AA H2 is independently selected from the group consisting of D-pip, D-nal, D-trp, D-bta, and D-phe. In a specific embodiment, D-AA H1 or D-AA H2 is D-nal. In other specific embodiments, D-AA H1 is D-nal. In some embodiments, each of L-AA H1 and L-AA H2 is independently selected from the group consisting of L-Pip, L-Nal, L-Trp, L-Bta, and L-Phe. In a specific embodiment, L-AA H1 and L-AA H2 Each of which is L-Nal. In other specific embodiments, L-AA H1 is L-Nal. The compounds described herein can be prepared in a variety of ways known to those of ordinary skill in the art of organic synthesis or by variations thereof as understood by those of ordinary skill in the art. The compounds described herein can be prepared from readily available starting materials. The optimal reaction conditions can vary depending on the specific reactants or solvents used, but such conditions can be determined by those of ordinary skill in the art. Variations of the compounds described herein include the addition, deletion, or movement of various components described for each compound. Similarly, when one or more chiral centers are present in the molecule, the chirality of the molecule can be changed. In addition, compound synthesis can involve the protection and deprotection of various chemical groups. The use of protection and deprotection and the selection of appropriate protecting groups can be determined by those of ordinary skill in the art. For protecting group chemistry, see, for example, Wuts and Greene, Protective Groups in Organic Synthesis, 4th Ed., Wiley & Sons, 2006, which is incorporated herein by reference in its entirety. Starting materials and reagents for the preparation of the disclosed compounds and compositions are available from commercial suppliers such as Aldrich Chemical Co., (Milwaukee, WI), Acros Organics (Morris Plains, NJ), Fisher Scientific (Pittsburgh, PA), Sigma (St.Louis, MO), Pfizer (New York, NY), GlaxoSmithKline (Raleigh, NC), Merck (Whitehouse Station, NJ), Johnson & Johnson (New Brunswick, NJ), Aventis (Bridgewater, NJ), AstraZeneca (Wilmington, DE), Novartis (Basel, Switzerland), Wyeth (Madison, NJ), Bristol-Myers-Squibb (New York, NY), Roche (Basel, Switzerland), Lilly (Indianapolis, IN), Abbott (Abbott Park, IL), Schering Plough (Kenilworth, NJ), or Boehringer Ingelheim (Ingelheim, Germany), or may be prepared by methods known to those of ordinary skill in the art following procedures described in the references, such as Fieser and Fieser’s Reagents for Organic Synthesis, Volumes 1-17 (John Wiley and Sons, 1991); Rodd’s Chemistry of Carbon Compounds, Volumes 1-5 and Supplementals (Elsevier Science Publishers, 1989); Organic Reactions, Volumes 1-40 (John Wiley and Sons, 1991); March’s Advanced Organic Chemistry, (John Wiley and Sons, 4th Edition); and Larock’s Comprehensive Organic Transformations (VCH Publishers Inc., 1989). Other materials such as pharmaceutical carriers disclosed herein may be obtained from commercial sources. The reactions to produce the compounds described herein can be carried out in a solvent, which can be selected by one of ordinary skill in the art of organic synthesis. The solvent can be substantially non-reactive with the starting materials (reactants), intermediates, or products under the conditions of the reaction, i.e., temperature and pressure. The reaction can be carried out in one solvent or a mixture of more than one solvent. The formation of the product or intermediate can be monitored according to any suitable method known in the art. For example, the formation of the product can be monitored by spectroscopic means such as nuclear magnetic resonance spectroscopy (e.g., 1 H or 13 C), infrared spectroscopy, spectrophotometry (e.g., UV-visible), or mass spectrometry, or by chromatography such as high performance liquid chromatography (HPLC) or thin layer chromatography. The disclosed compounds can be prepared by solid phase peptide synthesis, in which the amino acid α-N-terminus is protected by an acid or base protecting group. These protecting groups should have the property of being stable to the conditions for peptide bond formation, while being easily removable without destroying the growing peptide chain or racemization of any chiral centers contained therein. Suitable protecting groups are 9-fluorenylmethyloxycarbonyl (Fmoc), tert-butyloxycarbonyl (Boc), benzyloxycarbonyl (Cbz), biphenylisopropyloxycarbonyl, tert-pentyloxycarbonyl, isobornyloxycarbonyl, α,α-dimethyl-3,5-dimethoxybenzyloxycarbonyl, o-nitrophenylsulfenyl, 2-cyano-tert-butyloxycarbonyl, and the like. For the synthesis of the disclosed compounds, the 9-fluorenylmethyloxycarbonyl (Fmoc) protecting group is particularly preferred. Other preferred side chain protecting groups are: for side chain amines such as lysine and arginine, 2,2,5,7,8-pentamethyl 完-6-sulfonyl (pmc), nitro, p-toluenesulfonyl, 4-methoxybenzene-sulfonyl, Cbz, Boc, and adamantyloxycarbonyl; for tyrosine, benzyl, o-bromobenzyloxy-carbonyl, 2,6-dichlorobenzyl, isopropyl, tert-butyl (t-Bu), cyclohexyl, cyclopentyl, and acetyl (Ac); for serine, tert-butyl, benzyl, and tetrahydropyranyl; for histidine, triphenylmethyl, benzyl, Cbz, p-toluenesulfonyl, and 2,4-dinitrophenyl; for tryptophan, formyl; for aspartic acid and glutamic acid, benzyl and tert-butyl; and for cysteine, triphenylmethyl (trityl). In the solid-phase peptide synthesis method, the α-C-terminal amino acid is attached to a suitable support or resin. Suitable supports for the above synthesis are materials that are inert to the reagents and reaction conditions of the stepwise condensation-deprotection reaction and insoluble in the medium used. Supports for the synthesis of α-C-terminal carboxyl peptides are 4-hydroxymethylphenoxymethyl-copoly(styrene-1% divinylbenzene) or 4-(2',4'-dimethoxyphenyl-Fmoc-aminomethyl)phenoxyacetamidoethyl resin available from Applied Biosystems (Foster City, Calif.). The α-C-terminal amino acid is coupled to the resin by: N,N'-dicyclohexylcarbodiimide (DCC), N,N'-diisopropylcarbodiimide (DIC) or O-benzotriazol-1-yl-N,N,N',N'-tetramethyluronium hexafluorophosphate (HBTU), with or without 4-dimethylaminopyridine (DMAP), 1-hydroxybenzotriazole (HOBT), benzotriazol-1-yloxy-tris(dimethylamino)phosphonium hexafluorophosphate (BOP) or bis(2-oxo-3- in the presence of (azolidinyl)phosphine chloride (BOPCl), at a temperature between 10 °C and 50 °C in a solvent such as dichloromethane or DMF, for a coupling of about 1 to about 24 hours. When the support system is 4-(2',4'-dimethoxyphenyl-Fmoc-aminomethyl)phenoxy-acetamidoethyl resin, the Fmoc group is first cleaved with a secondary amine (preferably piperidine), and then coupled to the α-C-terminal amino acid as described above. One method for coupling to the deprotected 4-(2',4'-dimethoxyphenyl-Fmoc-aminomethyl)phenoxy-acetamidoethyl resin is O-benzotriazol-1-yl-N,N,N',N'-tetramethyluronium hexafluorophosphate (HBTU, 1 equiv.) and 1-hydroxybenzotriazole (HOBT, 1 equiv.) in DMF. The coupling of successive protected amino acids can be carried out in an automated peptide synthesizer. In one example, the α-N-terminus of the amino acids of the growing peptide chain is protected with Fmoc. Removal of the α-N-terminal side Fmoc protecting group of the growing peptide is accomplished by treatment with a secondary amine (preferably piperidine). Each protected amino acid is then introduced in about 3-fold molar excess, and the coupling is preferably carried out in DMF. The coupling agent can be O-benzotriazol-1-yl-N,N,N',N'-tetramethyluronium hexafluorophosphate (HBTU, 1 equiv.) and 1-hydroxybenzotriazole (HOBT, 1 equiv.). At the end of solid-phase synthesis, the polypeptide is removed from the resin and deprotected either sequentially or in a single operation. Removal of the polypeptide and deprotection can be accomplished in a single operation by treating the resin-bound polypeptide with a cleavage reagent containing anisole, water, ethanedithiol, and trifluoroacetic acid. In the case where the α-C-terminus of the polypeptide is an alkylamide, the resin is cleaved by aminolysis with an alkylamine. Alternatively, the peptide can be removed, for example, by transesterification with methanol, followed by aminolysis or direct deacylation. The protected peptide can be purified at this time or used directly in the next step. Removal of side-chain protecting groups can be accomplished using the cleavage cocktails described above. The fully deprotected peptide can be purified by a series of chromatographic steps employing any or all of the following types: ion exchange on a weakly basic resin (acetate form); hydrophobic adsorption chromatography on unmodified polystyrene-divinylbenzene (e.g., Amberlite XAD); silica gel adsorption chromatography; ion exchange chromatography on carboxymethyl cellulose; partition chromatography, for example, on Sephadex G-25, LH-20, or countercurrent distribution; high performance liquid chromatography (HPLC), particularly reverse-phase HPLC on octyl- or octadecylsilyl-silica-bonded phase column packings. Method of use Also provided herein are methods of using the compounds or compositions described herein. Also provided herein are methods for treating a disease or condition in a subject in need thereof, the method comprising administering to the subject an effective amount of any of the compounds or compositions described herein. Also provided herein are methods of treating cancer in a subject. Such methods include administering to the subject an effective amount of one or more of the compounds or compositions described herein, or a pharmaceutically acceptable salt thereof. The compounds and compositions or pharmaceutically acceptable salts thereof described herein can be used to treat cancer in humans (e.g., pediatric and geriatric populations) and animals (e.g., veterinary applications). The disclosed methods optionally can include identifying a patient in need or likely to be in need of treatment for cancer. Examples of types of cancer that can be treated by the compounds and compositions described herein include bladder cancer, brain cancer, breast cancer, colorectal cancer, cervical cancer, gastrointestinal cancer, genitourinary cancer, head and neck cancer, lung cancer, ovarian cancer, pancreatic cancer, prostate cancer, kidney cancer, skin cancer, and testicular cancer. Further examples include cancer of the anus, bile duct, bone, bone marrow, bowel (including colon and rectum), eye, gallbladder, kidney, mouth, larynx, esophagus, stomach, testis, cervix, mesothelioma, neuroendocrine, penis, skin, spinal cord, thyroid, vagina, vulva, uterus, liver, muscle, blood cells (including lymphocytes and other immune system cells), and / or tumors. Further examples of cancer that can be treated by the compounds and compositions described herein include carcinoma, Karposi's sarcoma, melanoma, mesothelioma, soft tissue sarcoma, pancreatic cancer, lung cancer, leukemia (acute lymphoblastic, acute myeloid, chronic lymphocytic, chronic myeloid, and others), and lymphoma (Hodgkin's and non-Hodgkin's), and multiple myeloma. The methods of treating or preventing cancer described herein can further include treating with one or more additional agents (e.g., anticancer agents or ionizing radiation). The one or more additional agents and the compounds or compositions or pharmaceutically acceptable salts thereof as described herein can be administered in any order, including simultaneously, and in a sequential order with a temporal interval of up to several days. The methods also can include administering more than a single dose of the one or more additional agents and / or the compounds or compositions or pharmaceutically acceptable salts thereof as described herein. Administration of the one or more additional agents and the compounds or compositions or pharmaceutically acceptable salts thereof as described herein can be by the same or different routes. When treating with one or more additional agents, the compounds or compositions or pharmaceutically acceptable salts thereof as described herein can be combined into a pharmaceutical composition that includes the one or more additional agents. For example, a compound or composition or a pharmaceutically acceptable salt thereof as described herein can be combined with an additional anti-cancer agent into a pharmaceutical composition, the additional anti-cancer agent such as 13-cis-retinoic acid, 2-amino-6-mercaptopurine, 2-CdA, 2-chlorodeoxyadenosine, 5-fluorouracil, 6-thioguanine, 6-mercaptopurine, Accutane, actinomycin-D, doxorubicin, Adrucil, Agrylin, Ala-Cort, aldesleukin, alemtuzumab, acitretin, Alkaban-AQ, Alkeran, all-trans-retinoic acid, alpha interferon, hexamethylmelamine, methotrexate, amifostine, aminoglutethimide, anagrelide, Anandron, anastrozole, cytarabine, Aranesp, Aredia, Arimidex, Aromasin, arsenic trioxide, asparaginase, ATRA, Avastin, BCG, BCNU, bevacizumab, bexarotene, bicalutamide, BiCNU, Blenoxane, bleomycin, bortezomib, busulfan, Busulfex, C225, calcium folinate, Campath, Camptosar, irinotecan, capecitabine, Carac, carboplatin, carmustine, carmustine wafer, Casodex, CCNU, CDDP, CeeNU, Cerubidine, cetuximab, chlorambucil, cisplatin, citrovorum factor, cladribine, cortisone, Cosmegen, CPT-11, cyclophosphamide, Cytadren, cytarabine, liposomal cytarabine, Cytosar-U, Cytoxan, dacarbazine, actinomycin D, Darbepoetinalfa, Daunomycin, Daunorubicin, Daunorubicin Hydrochloride, Daunorubicin Liposome, DaunoXome, Decadron, δ-Cortef, Deltasone, Denileukin-Diftitox, DepoCyt, Dexamethasone, Dexamethasone Acetate, Dexamethasone Sodium Phosphate, Dexasone, Dexrazoxane, DHAD, DIC, Diodex, Docetaxel, Doxil, Doxorubicin, Doxorubicin Liposome, Droxia, DTIC, DTIC-Dome, Duramycin, Efudex, Eligard, Elence, Oxaliplatin, Esberitox, Emcyt, Epirubicin, Epogen, Erbitux, Erwinia L-Asparaginase, Estramustine, Ethyol, Famotidine, Etoposide, Etoposide Phosphate, Eulexin, Evista, Exemestane, Faslodex, Faldostat, Lipiodol, Filgrastim, Floxuridine, Fludara, Fludarabine, Fluoroplex, Fluorouracil, Fluorouracil (Cream), Fluoxymesterone, Flutamide, Folinic Acid, FUDR, Fulvestrant, G-CSF, Gefitinib, Gemcitabine, Gemtuzumab Ozogamicin, Gemzar, Gleevec, Lupron, LupronDepot, Matulane, Maxidex, methylbis(2-chloroethyl)amine, methylbis(2-chloroethyl)amine hydrochloride, Medrol, Medrol, Megace, megestrol acetate, melphalan, mercaptopurine, mesna, Mesnex, methotrexate, methotrexate sodium, methylprednisolone, Mylocel, letrozole, Neosar, Neulasta, Nimotuzumab, Youbaojin, nilandron, nilutamide, nitrogen mustard, Novaldex, Novantrone, octreotide, octreotide acetate, Oncospar, vincristine, Ontak, Onxal, Oprelvekin, Orapred, Orasone, oxaliplatin, paclitaxel, pamidronate, Panretin, Paraplatin, Pediapred, PEG interferon, pegaspargase, pegfilgrastim, PEG-INTRON, PEG-L-asparaginase, phenylalanine mustard, Platinol, Platinol-AQ, prednisone, prednisolone, Prelone, procarbazine, PROCRIT, Puri Jing, Prophane 20 with carmustine implant, Purinethol, raloxifene, Rheumatrex, Rituxan, rituximab, Roveron-A (interferon α-2a), Rubex, rubidomycin hydrochloride, Sandostatin, Sandostatin LAR, sargramostim, Solu-Cortef, Solu-Medrol, STI-571, streptozocin, tamoxifen, targretin, taxol, Kailaiyi, Temodar, temozolomide, teniposide, TESPA, thalidomide, thalidomide, TheraCys, thioguanine, thioguanine tablets, thiofosfamide, Thioplex, thiotepa, TICE, Toposar, topotecan, toremifene, trastuzumab, tretinoin, Trexall, Trisenox, TSPA, VCR, Velban, Velcade, VePesid, Vesanoid, Viadur, vinblastine, vinblastine sulfate, Vincasar Pfs, vincristine, vinorelbine, vinorelbine tartrate, VLB, VP-16,威猛, Jieliu Da, Zanosar, Ze Wa Ling, Zinecard,诺雷德, zoledronic acid, Zometa, Gliadel wafers, Glivec, GM-CSF, goserelin, granulocyte colony-stimulating factor, fluoxymesterone, Herceptin, Hexadrol, Hexalen, hexamethylmelamine, HMM, Aikangding, Aizhi, hydrocortisone acetate, hydrocortisone, hydrocortisone sodium phosphate, hydrocortisone sodium succinate, hydrocortisone phosphate, hydroxyurea, Ibritumomab,替伊莫单抗, idarubicin, idarubicin, Ifex, IFN-α,依弗醯胺, IL It should be noted that there are some Chinese names in the original text that may not have standard English translations or may be incorrect. The above translation tries to maintain the original content as much as possible while translating the known parts. If there are specific requirements for the translation of certain terms, it may need to be adjusted according to the actual situation.2. IL-11, imatinib mesylate, temozolomide, interferon α, interferon α-2b (PEG conjugate), interleukin 2, interleukin-11, Intron A (interferon α-2b), folinic acid, chlorambucil, Leukine, leuprorelin, vincristine, vinblastine, liposomal Ara-C, liquid Pred, lomustine, L-PAM, L-sarcolysin, Meticorten, mitomycin, mitomycin-C, mitoxantrone, M-prednisone, MTC, MTX, Mustargen, nitrogen mustard, mutamycin, Myleran, Iressa, irinotecan, isotretinoin, Kidrolase, Lanacort, L-asparaginase, and LCR. Additional anti-cancer agents may also include biological agents such as, for example, antibodies. Many tumors and cancers have viral genomes present in the tumor or cancer cells. For example, Epstein-Barr virus (EBV) is associated with some mammalian malignancies. The compounds disclosed herein may also be used alone or in combination with anti-cancer or anti-viral agents such as ganciclovir, azidothymidine (AZT), lamivudine (3Tc), etc., to treat patients infected with viruses that can cause cellular transformation and / or to treat patients with tumors or cancers associated with the presence of viral genomes in cells. The compounds disclosed herein may also be used in combination with virus-based tumor disease therapies. Methods of killing target tumor cells are also described herein. The method includes contacting the tumor cells with an effective amount of a compound or composition as described herein, and optionally includes the step of irradiating the tumor cells with an effective amount of ionizing radiation. In addition, methods of radiotherapy of tumors are provided herein. These methods include contacting the tumor cells with an effective amount of a compound or composition as described herein, and irradiating the tumor with an effective amount of ionizing radiation. As used herein, the term ionizing radiation refers to radiation that includes particles or photons having sufficient energy or capable of producing sufficient energy via nuclear interactions to produce ionization. Examples of ionizing radiation are x-radiation. An effective amount of ionizing radiation is an ionizing radiation dose that produces an increase in cell injury or death when administered in combination with the compounds described herein. Ionizing radiation can be delivered according to methods known in the art, including administration of radiolabeled antibodies and radioisotopes. The methods and compounds described herein can be used for both prophylactic and therapeutic treatment. As used herein, the term "treating" or "treatment" includes prevention; delaying the onset; reducing, eradicating, or delaying the worsening of post-onset symptoms or signs; and preventing recurrence. For prophylactic use, a therapeutically effective amount of a compound and composition or a pharmaceutically acceptable salt thereof as described herein is administered to a subject before the onset of disease (e.g., before overt cancer signs), during the early onset period (e.g., the initial signs and symptoms of cancer appear), or after the definite development of cancer. Prophylactic administration can occur from days to years before the manifestation of infectious symptoms. Prophylactic administration can be used for, for example, chemopreventive treatment of subjects presenting with precancerous lesions, those diagnosed with early-stage malignancies, and subgroups (e.g., families, ethnic groups, and / or occupations) susceptible to a particular cancer. Therapeutic treatment involves administering to a subject a therapeutically effective amount of a compound and composition or a pharmaceutically acceptable salt thereof as described herein after cancer diagnosis. In some examples of methods for treating cancer or tumors in a subject, the compound or composition administered to the subject can comprise a therapeutic moiety, which can comprise a targeting moiety that can act as an inhibitor against Ras (e.g., K-Ras), PTP1B, Pin1, Grb2 SH2, or a combination thereof. The disclosed subject matter is also directed to methods for treating a subject having a metabolic disorder or condition. In one embodiment, an effective amount of one or more compounds or compositions disclosed herein is administered to a subject having a metabolic disorder and in need of such treatment. In some examples, the metabolic disorder can comprise type II diabetes. In some examples of methods for treating a metabolic disorder in a subject, the compound or composition administered to the subject can comprise a therapeutic moiety, which can comprise a targeting moiety that can act as an inhibitor against PTP1B. In one particular example of this method, the subject is obese and the method comprises treating the subject's obesity by administering a composition disclosed herein. The disclosed subject matter is also directed to methods for treating a subject having an immune disorder or condition. In one embodiment, an effective amount of one or more compounds or compositions disclosed herein is administered to a subject having an immune disorder and in need of such treatment. In some examples of methods for treating an immune disorder in a subject, the compound or composition administered to the subject can comprise a therapeutic moiety, which can comprise a targeting moiety that can act as an inhibitor against Pin1. The disclosed subject matter is also directed to methods for treating a subject having an inflammatory disorder or condition. In one embodiment, an effective amount of one or more compounds or compositions disclosed herein is administered to a subject having an inflammatory disorder and in need of such treatment. The disclosed subject matter also relates to methods for treating a subject having cystic fibrosis. In one embodiment, an effective amount of one or more of the compounds or compositions disclosed herein is administered to a subject having cystic fibrosis and in need of such treatment. In some examples of methods for treating a subject's cystic fibrosis, the compound or composition administered to the subject may comprise a therapeutic moiety, which may comprise a targeting moiety that can act as an inhibitor against CAL PDZ. In some embodiments, the CPPs disclosed herein can be used to detect or diagnose a disease or condition in a subject. For example, a CPP may comprise a targeting moiety and / or a detectable moiety that can interact with a target such as a tumor. Compositions, Formulations, and Methods of Administration In vivo applications of the disclosed compounds and compositions containing them can be accomplished by any suitable methods and techniques currently or prospectively known to those of ordinary skill in the art. For example, the disclosed compounds can be formulated into a physiologically or pharmaceutically acceptable form and administered by any suitable route known in the art, including, for example, oral, nasal, rectal, topical, and parenteral routes of administration. As used herein, the term parenteral includes administration by, for example, subcutaneous, intradermal, intravenous, intramuscular, intraperitoneal, and intrasternal injection. Administration of the disclosed compounds or compositions can be a single administration, or can be readily determined by those of ordinary skill in the art to be administered continuously or at different intervals. The compounds disclosed herein and compositions containing them can also be administered using liposome technology, sustained-release capsules, implantable pumps, and biodegradable containers. These delivery methods can advantageously provide a uniform dosage over an extended period of time. The compounds can also be administered in the form of their salt derivatives or crystalline forms. The compounds disclosed herein can be prepared according to known methods for preparing pharmaceutically acceptable compositions. Formulations are described in detail in some sources well known and readily available to those of ordinary skill in the art. For example, Remington’s Pharmaceutical Science by E.W. Martin (1995) describes formulations that can be used in connection with the disclosed methods. Generally, the compounds disclosed herein can be formulated such that an effective amount of the compound is combined with a suitable carrier to facilitate the effective administration of the compound. The compositions used can also be presented in various forms. These include, for example, solid, semi-solid, and liquid dosage forms such as tablets, pills, powders, liquid solutions or suspensions, suppositories, solutions for injection and infusion, and sprays. The preferred form depends on the intended mode of administration and the therapeutic application. The compositions also preferably include conventional pharmaceutically acceptable carriers and diluents known to those of ordinary skill in the art. Examples of carriers or diluents used with the compounds include ethanol, dimethyl sulfoxide, glycerol, alumina, starch, saline, and equivalent carriers and diluents. To provide for the administration of such doses for the desired therapeutic treatment, the compositions disclosed herein can advantageously contain one or more of the subject compounds in an amount ranging from about 0.1% to 100% based on the total weight of the composition including the carrier or diluent. Formulations suitable for administration include, for example, sterile aqueous injection solutions which may contain antioxidants, buffers, bacteriostats, and solutes that render the formulation isotonic with the blood of a predetermined recipient; and aqueous and non-aqueous sterile suspensions which may include suspending and thickening agents. The formulations can be presented in unit-dose or multi-dose containers, for example, sealed ampoules and vials, and can be stored in a freeze-dried (lyophilized) state that requires only a sterile liquid carrier, for example, water for injection, to be reconstituted before use. The temporary injection solutions and suspensions can be prepared from sterile powders, granules, tablets, etc. It should be understood that in addition to the ingredients specifically mentioned above, the compositions disclosed herein can include other agents conventional in the art, taking into account the type of formulation under discussion. The compounds and compositions containing them disclosed herein can be delivered to cells either by direct contact with the cells or by carrier means. Carrier means for delivering the compounds and compositions to cells are known in the art and include, for example, encapsulating the composition in lipid vesicles. Another means for delivering the compounds and compositions disclosed herein to cells involves conjugating the compound to a protein or nucleic acid that is targeted to the target cell. U.S. Patent No. 6,960,648 and U.S. Application Publication Nos. 20030032594 and 20020120100 disclose amino acid sequences that can be conjugated to another composition and permit the composition to translocate across biological membranes. U.S. Application Publication No. 20020035243 also describes compositions for transporting biological moieties across cell membranes for intracellular delivery. The compounds can also be incorporated into polymers, examples of which include poly(D-L lactide-co-glycolide) polymers for intracranial tumors; poly[bis(p-carboxyphenoxy)propane:sebacic acid] (20:80 molar ratio) (as used in Gliadel); chondroitin; chitin; and polyglucosamine. For the treatment of tumor disorders, the compounds disclosed herein can be administered to a patient in need of treatment in combination with other anti-tumor or anti-cancer substances and / or with radiation and / or photodynamic therapy and / or with surgical treatment for removing the tumor. These other substances or treatments can be given simultaneously with or at different times from the compounds disclosed herein. For example, the compounds disclosed herein can be used in combination with mitotic inhibitors such as paclitaxel or vinblastine, alkylating agents such as cyclophosphamide or ifosfamide, antimetabolites such as 5-fluorouracil or hydroxyurea, DNA intercalating agents such as doxorubicin or bleomycin, topoisomerase inhibitors such as etoposide or camptothecin, anti-angiogenic agents such as angiostatin, anti-estrogens such as tamoxifen, and / or other anti-cancer drugs or antibodies such as, for example, Gleevec (Novartis Pharmaceuticals Corporation) and Herceptin (Genentech, Inc.), respectively, or immunotherapeutic agents such as ipilimumab and bortezomib. In certain instances, the compounds and compositions disclosed herein may be administered locally, optionally in combination with a pharmaceutically acceptable carrier such as an inert diluent, at one or more anatomical sites such as sites of unwanted cell growth, such as tumor sites or benign skin growths, e.g., by injection or topical application to the tumor or skin growth. The compounds and compositions disclosed herein may be administered systemically, such as intravenously or orally, optionally in combination with a pharmaceutically acceptable carrier such as an inert diluent or an absorbable edible carrier for oral delivery. They may be enclosed in hard or soft shell gelatin capsules, compressed into tablets, or incorporated directly into the food of the patient's diet. For oral therapeutic administration, the active compound may be combined with one or more excipients and used in the form of ingestible tablets, buccal tablets, lozenges, capsules, elixirs, suspensions, syrups, wafers, aerosols, and the like. The disclosed compositions are bioavailable and may be orally delivered. Oral compositions may be tablets, lozenges, pills, capsules, and the like, and may also contain the following: binders such as acacia, gelatin, corn starch, or gelatin; excipients such as dicalcium phosphate; disintegrants such as corn starch, potato starch, alginic acid, and the like; lubricants such as magnesium stearate; and sweetening agents such as sucrose, fructose, lactose, or aspartame or flavoring agents such as peppermint, wintergreen oil, or cherry flavor may be added. When the unit dosage form is a capsule, it may contain a liquid carrier such as a vegetable oil or polyethylene glycol in addition to the materials of the above types. Various other materials may be present as coatings or otherwise modify the physical form of the solid unit dosage form. For example, tablets, pills, or capsules may be coated with gelatin, wax, shellac, or sugar and the like. Syrups or elixirs may contain the active compound, sucrose or fructose as a sweetening agent, methyl and propyl parabens as preservatives, dyes, and flavoring agents such as cherry or orange flavor. Of course, any material used in the preparation of any unit dosage form should be pharmaceutically acceptable and the amounts employed should be substantially non-toxic. In addition, the active compound may be incorporated into sustained release formulations and devices. The compounds and compositions disclosed herein, including their pharmaceutically acceptable salts or prodrugs, may be administered by intravenous, intramuscular, or intraperitoneal infusion or injection. Solutions of the active agent or its salts may be prepared in water, optionally mixed with a non-toxic surfactant. Dispersions may also be prepared in glycerol, liquid polyethylene glycols, triacetin, and mixtures thereof and in oils. Under ordinary storage conditions and use, these preparations may contain preservatives to prevent the growth of microorganisms. Pharmaceutical dosage forms suitable for injection or infusion may include sterile aqueous solutions or dispersions or sterile powders containing the active ingredient, which are adapted for the extemporaneous preparation of sterile injectable or infusible solutions or dispersions optionally enclosed in liposomes. The final dosage form should be sterile, fluid, and stable under the conditions of manufacture and storage. The liquid carrier or vehicle can be a solvent or a liquid dispersion medium, including, for example, water, ethanol, polyols (such as glycerol, propylene glycol, liquid polyethylene glycol, and the like), vegetable oils, non-toxic glycerides, and suitable mixtures thereof. Appropriate fluidity can be maintained, for example, by forming liposomes, by maintaining the desired particle size in the case of a dispersion, or by using surfactants. Optionally, the prevention of microbial action can be achieved by various other antibacterial and antifungal agents such as parabens, chlorobutanol, phenol, sorbic acid, thimerosal, and the like. In many cases, it is preferred to include isotonic agents such as sugars, buffers, or sodium chloride. Prolonged absorption of injectable compositions can be achieved by including agents that delay absorption such as aluminum monostearate and gelatin. The preparation of a sterile injectable solution is achieved by incorporating the required amount of the compounds and / or agents disclosed herein into a suitable solvent optionally containing various other ingredients listed above, followed by filtration sterilization. In the case of a sterile powder for the preparation of a sterile injectable solution, the preferred methods of preparation are vacuum drying and lyophilization techniques, which yield a powder of the active ingredient plus any additional desired ingredients present in the previously filtered and sterilized solution. For topical administration, the compounds and agents disclosed herein can be administered as a liquid or a solid. However, it is generally desired to combine them as a composition with a dermatologically acceptable carrier (which can be solid or liquid) for topical administration to the skin. The compounds and agents and compositions disclosed herein can be topically applied to the skin of a subject to reduce the size of a malignant or benign growth (and can include complete removal), or to treat an infected site. The compounds and agents disclosed herein can be directly applied to the growth or infected site. Preferably, the compounds and agents are administered to the growth or infected site in a formulation such as an ointment, cream, lotion, solution, tincture, or the like. Solid carriers that can be used include finely divided solids such as talc, clay, microcrystalline cellulose, silica, alumina, and the like. Liquid carriers that can be used include water, alcohols or glycols, or water-alcohol / glycol blends, in which the compounds can be dissolved or dispersed at an effective level, optionally with the aid of a non-toxic surfactant. Adjuvants such as fragrances and additional antibacterial agents can be added to optimize the properties for a given use. The resulting liquid composition can be applied from an absorbent pad, used for impregnating bandages and other dressings, or sprayed onto the affected area using, for example, a pump-type or aerosol sprayer. Thickeners such as synthetic polymers, fatty acids, fatty acid salts and esters, fatty alcohols, modified celluloses or modified mineral materials can also be used with a liquid carrier to form a spreadable paste, gel, ointment, soap, and the like for direct application to the skin of a user. The useful dosage of the compounds, agents and pharmaceutical compositions disclosed herein can be determined by comparing their in vitro activity and in vivo activity in animal models. Methods for extrapolating effective dosages in mice and other animals to humans are known in the art. The dosage range for administration of the composition is a range of dosages large enough to produce the desired effect that can affect the symptoms or condition. The dosage should not be so large as to cause adverse reactions such as unwanted cross-reactions, allergic reactions, and the like. Generally, the dosage will vary with the age, condition, sex and disease scope of the patient and can be determined by those of ordinary skill in the art. The dosage can be adjusted by an individual physician depending on any contraindications. The dosage can vary and can be administered one or more times per day for one or more days. Also disclosed are pharmaceutical compositions comprising a combination of a compound disclosed herein and a pharmaceutically acceptable carrier. Pharmaceutical compositions adapted for oral, topical or parenteral administration and comprising an amount of the compound constitute a preferred aspect. The dosage administered to a patient, particularly a human, should be sufficient to achieve a therapeutic response in the patient within a reasonable period of time, without lethal toxicity, and preferably causing adverse reactions or morbidity not greater than an acceptable level. Those of ordinary skill in the art will recognize that the dosage will depend on a variety of factors including the condition (health) of the subject, the weight of the subject, the type of concomitant treatment (if any), the frequency of treatment, the proportion of treatment, and the severity and stage of the pathological condition. Also disclosed are kits comprising a compound disclosed herein in one or more containers. The disclosed kits can optionally include a pharmaceutically acceptable carrier and / or diluent. In one embodiment, the kit includes one or more other components, additives, or adjuvants as described herein. In another embodiment, the kit includes one or more anti-cancer agents, such as those described herein. In one embodiment, the kit includes instructions or packaging materials describing how to administer the compounds or compositions of the kit. The containers of the kit can be of any suitable material, such as glass, plastic, metal, etc. and of any suitable size, shape, or configuration. In one embodiment, the compound and / or agent disclosed herein is provided in the kit as a solid, such as in the form of tablets, pills, or powders. In another embodiment, the compound and / or agent disclosed herein is provided in the kit as a liquid or solution. In one embodiment, the kit contains an ampoule or syringe containing the compound and / or agent disclosed herein in liquid or solution form. Example Example 1. CPP synthesis The peptide was synthesized using standard Fmoc chemistry on Rink amide resin LS (0.2 mmol / g). The general coupling reaction contained 5 equivalents of Fmoc - amino acid, 5 equivalents of 2-(7 - azabenzotriazol - 1 - yl)-1,1,3,3 - tetramethyluronium hexafluorophosphate (HATU), and 10 equivalents of diisopropylethylamine (DIPEA), and was allowed to proceed for 75 min under mixing. After addition of the final (N - terminal) residue, the allyl group on the C - terminal Glu residue was removed by treatment with anhydrous DCM (3 × 15 min) containing Pd(PPh 3 ) 4 , phenylsilane (0.1 and 10 equivalents respectively). The N - terminal Fmoc group was removed by treatment with DMF containing 20% piperidine, and the peptide was cyclized by treatment with DMF containing benzotriazol - 1 - yloxy - tris - pyrrolidinophosphonium hexafluorophosphate (PyBOP) / HOBt / DIPEA (5, 5, and 10 equivalents) for 3 h. The peptide was deprotected and released from the resin by treatment with 82.5:5:5:5:2.5 (v / v) TFA / anisole / water / phenol / ethanedithiol for 2 h. The peptide was triturated with cold diethyl ether (3x) and purified by reverse - phase HPLC on a C 18 column. The product purity (>98%) was evaluated by reverse - phase HPLC equipped with an analytical C 18 column. The authenticity of each peptide was confirmed by MALDI - TOF mass spectrometry. To produce the fluorescently labeled peptide, N e - 4 - methoxytrityl - L - lysine was added to the C - terminus prior to peptide synthesis. After completion of solid - phase synthesis but before cleavage, the lysine side chain was selectively deprotected using DCM containing 1% (v / v) TFA. The resin was incubated overnight in DMF with 5 equivalents of the reactive fluorescent labeling reagent (fluorescein isothiocyanate, Lissamine rhodamine B sulfonyl chloride, or naphthofluorescein succinimidyl ester) and 5 equivalents of DIPEA. The labeled peptide was deprotected, triturated, purified, and analyzed by MALDI - TOF MS as described above. Example 2. Cellular uptake efficiency To determine the cellular uptake efficiency of the CPPs disclosed herein, HeLa cells were cultured in 12 - well plates (1.5 × 10 per well 5The cells were incubated overnight. The cells were incubated with 5 mM naphthofluorescein (NF)-labeled peptide in cell medium for 2 h. At the end of incubation, the cells were washed twice with DPBS, detached from the plate with 0.25% trypsin, diluted into clear DMEM, pelleted at 250 g for 5 min, washed twice with DPBS, resuspended in DPBS, and analyzed on a BD FACS LSR II flow cytometer. For the NF-labeled peptide, 633-nm laser excitation was used and fluorescence emission was analyzed in the APC channel. The absolute cell uptake efficiency was determined by comparing the concentration of the CPP in the cytosol (via fluorescence intensity) with the concentration in the extracellular medium. The relative cell uptake efficiency was determined by comparing the cytosolic concentration of the CPP with the cytosolic concentration of the control CPP cyclo(FФRRRRQ) (SEQ ID NO:10). From the foregoing discussion, it will be appreciated that the present invention may be embodied in many forms, including but not limited to the following: Example 1. A cyclic peptide according to one of formulas I-A to I-E: , , , , or wherein AA 1 , AA 2 , AA 3 , AA 4 , AA 5 , AA 6 , AA 7 , AA 8 , AA 9 , and AA 10 each, when present, is independently selected from amino acids; and wherein: AA 1 , AA 2 , AA 3 , AA 4 , AA 5 , AA 6 , AA 7 , AA 8 , AA 9 , or AA 10 When two or three of them are present, they are arginine, and the remaining amino acids are amino acids other than arginine; and AA 1 , AA 2 , AA 3 , AA 4 , AA 5 , AA 6 , AA 7 , AA 8 , AA 9 , or AA 10At least two of them are independently hydrophobic amino acids when present. Example 2. A cyclic peptide as in Example 1, wherein each hydrophobic amino acid is independently selected from the group consisting of phenylglycine, leucine, isoleucine, norleucine, methionine, phenylalanine, homophenylalanine, cyclohexylalanine, tyrosine, piperidine-2-carboxylate, tryptophan, proline, 3-(3-benzothienyl)-alanine, and naphthylalanine, each of which is optionally substituted with one or more substituents. Example 3. A cyclic peptide as in Example 1, wherein each hydrophobic amino acid is independently piperidine-2-carboxylate, naphthylalanine, tryptophan, 3-(3-benzothienyl)-alanine, or phenylalanine, each of which is optionally substituted with one or more substituents. Example 4. A cyclic peptide as in Example 1, wherein at least one hydrophobic amino acid has a hydrophobicity greater than or equal to that of phenylalanine. Example 5. A cyclic peptide as in Example 1, wherein at least two of the amino acids have relative chirality. Example 6. A cyclic peptide as in any one of Examples 1 to 5, wherein at least two of the amino acids have the same chirality. Example 7. A cyclic peptide as in any one of Examples 1 to 6, wherein one arginine is adjacent to a hydrophobic amino acid. Example 8. A cyclic peptide as in Example 7, wherein the arginine has the same chirality as the adjacent hydrophobic amino acid. Example 9. A cyclic peptide as in any one of Examples 1 to 8, wherein at least two arginines are adjacent to each other. Example 10. A cyclic peptide as in any one of Examples 1 to 9, wherein three arginines are adjacent to each other. Example 11. A cyclic peptide as in any one of Examples 1 to 10, wherein at least two hydrophobic amino acids are adjacent to each other. Example 12. A cyclic peptide as in any one of Examples 1 to 11, wherein at least three hydrophobic amino acids are adjacent to each other. Example 13. A cyclic peptide as in any one of Examples 1 to 12, wherein any four adjacent amino acids are AA H2 -AA H1 -R-r、AA H2 -AA H1 -r-R、R-r-AA H1 -AA H2 、or r-R-AA H1 -AA H2 ,wherein AA H1 and AA H2 each of which is independently a hydrophobic amino acid. Example 14. A cyclic peptide having a structure according to any one of Formulas II-A to II-D: , , and wherein: AA H1 and AA H2 each of which is independently a hydrophobic amino acid; AA U and AA Z is independently any amino acid each time it appears; and each AA U and each AA Z at most one of which is arginine; and wherein: each of m and n is independently a number from 0 to 6, provided that at least one of m or n is not 0 and the total number of amino acids is from 6 to 10. Example 15. A cyclic peptide as in Example 13 or 14, wherein AA H1 and AA H2 are independently piperidine-2-carboxylate, naphthylalanine, tryptophan, 3-(3-benzothienyl)-alanine, or phenylalanine, each of which is optionally substituted with one or more substituents. Example 16. A cyclic peptide as in any one of Examples 13 to 15, wherein AA H1 and AA H2 are independently hydrophobic amino acids having a hydrophobicity greater than or equal to that of phenylalanine. Example 17. A cyclic peptide as in any one of Examples 13 to 16, wherein AA H1 is naphthylalanine. Example 18. A cyclic peptide as in any one of Examples 13 to 17, wherein AA H1 and AA H2 are naphthylalanine. Example 19. A cyclic peptide as in any one of Examples 13 to 18, wherein AA H1 is a hydrophobic amino acid having a large solvent-accessible surface area (SASA) in the side chain. Example 20. A cyclic peptide as in Example 19, wherein the large SASA is at least about 200 Å 2 . Example 21. A cyclic peptide as in any one of Examples 13 to 20, wherein AA H2 has a side-chain SASA less than or equal to AA H1The hydrophobic amino acid of the SASA of the side chain. Example 22. A cyclic peptide as in any one of Examples 13 to 21, wherein when any AA U or any AA Z is a hydrophobic amino acid, the hydrophobic amino acid has a side chain with a SASA smaller than AA H1 Example 23. A cyclic peptide as in any one of Examples 13 to 22, wherein AA H1 and AA H2 have the same or opposite chirality. Example 24. The cyclic peptide as in Example 23, wherein AA H1 and AA H2 have opposite chirality. Example 25. A cyclic peptide as in any one of Examples 13 to 24, wherein AA H1 has the same chirality as the adjacent arginine. Example 26. A cyclic peptide as in any one of Examples 13 to 25, having one of the following sequences: AA H2 -AA H1 -R-r-R, AA H2 -AA H1 -R-r-r, AA H2 -AA H1 -r-R-R, AA H2 -AA H1 -r-R-r, R-R-r-AA H1 -AA H2 , r-R-r-AA H1 -AA H2 , r-r-R-AA H1 -AA H2 , or R-r-R-AA H1 -AA H2。 Example 27. The cyclic peptides of Examples 13 to 26 have one of the following sequences: AA H2 -LAA H1 -R-r-R, AA H2 -DAA H1 -r-R-r, r-R-r-DAA H1 -AA H2 、 or R-r-R-LAA H1 -AA H2Example 28. A cyclic peptide according to any one of Examples 1 to 27, having a relative cytosolic delivery efficiency in an amount in the range of about 50% to about 500% improvement compared to cyclo(FФRRRRQ) (SEQ ID NO:10). Example 29. A cyclic peptide according to Example 28, wherein the cyclic peptide has a relative cytosolic delivery efficiency in the range of about 175% to about 250% improvement compared to cyclo(FФRRRRQ) (SEQ ID NO:10). Example 30. A cyclic peptide according to Example 29, comprising the following sequence: FfFRrR (SEQ ID NO:131). Example 31. A cyclic peptide according to Example 28, wherein the cyclic peptide has a relative cytosolic delivery efficiency in the range of about 150% to about 400% improvement compared to cyclo(FФRRRRQ) (SEQ ID NO:10). Example 32. A cyclic peptide according to Example 31, comprising the following sequence: fFfrRr (SEQ ID NO:132). Example 33. A cyclic peptide according to Example 32, wherein the cyclic peptide has a cytosolic delivery efficiency in the range of about 75% to about 275% improvement compared to cyclo(FФRRRRQ) (SEQ ID NO:10). Example 34. A cyclic peptide according to Example 33, comprising the following sequence: fFfRrR (SEQ ID NO:133). Example 35. A cyclic peptide according to Example 28, wherein the cyclic peptide has a cytosolic delivery efficiency in the range of about 150% to about 250% improvement compared to cyclo(FФRRRRQ) (SEQ ID NO:10). Example 36. A cyclic peptide according to Example 35, comprising the following sequence: FfFrRr (SEQ ID NO:134). Example 37. A cyclic peptide according to Example 36, wherein the cyclic peptide has a cytosolic delivery efficiency in the range of about 200% to about 450% improvement compared to cyclo(FФRRRRQ) (SEQ ID NO:10). Example 38. A cyclic peptide according to Example 37, comprising the following sequence: fFɸrRr (SEQ ID NO:135). Example 39. A cyclic peptide according to Example 28, wherein the peptide has a cytosolic delivery efficiency in the range of about 250% to about 450% improvement compared to cyclo(FФRRRRQ) (SEQ ID NO:10). Example 40. A cyclic peptide according to Example 39, comprising the following sequence: fФfrRr (SEQ ID NO:136). Example 41. A cyclic peptide according to Formulae III-A to III-D: , , , or wherein: AA 1 , AA 2 , AA 3 , and AA 4 each of which is independently selected from amino acids; AA U and AA Z each occurrence is independently selected from amino acids; each of m and n is a number from 0 to 6, provided that at least one of m or n is not 0; X n is the cargo portion; L is the linker portion; wherein: AA 1 、AA 2 、AA 3 、AA 4 、each AA U 、and each AA Z two or three of which are arginine, and the remaining amino acids are amino acids other than arginine; AA 1 、AA 2 、AA 3 、AA 4 、each AA U 、and each AA Z at least two of which are independently hydrophobic amino acids; and wherein when X n is attached to AA uWhen, m is not 0. Example 42. A cyclic peptide as in Example 41, wherein each hydrophobic amino acid is independently selected from the group consisting of phenylglycine, leucine, isoleucine, norleucine, methionine, phenylalanine, homophenylalanine, cyclohexylalanine, tyrosine, piperidine-2-carboxylate, tryptophan, proline, 3-(3-benzothienyl)-alanine, and naphthylalanine, each of which is optionally substituted with one or more substituents. Example 43. A cyclic peptide as in Example 41, wherein each hydrophobic amino acid is independently piperidine-2-carboxylate, naphthylalanine, tryptophan, 3-(3-benzothienyl)-alanine, or phenylalanine, each of which is optionally substituted with one or more substituents. Example 44. A cyclic peptide as in Example 41, wherein at least one hydrophobic amino acid has a hydrophobicity greater than or equal to that of phenylalanine. Example 45. A cyclic peptide as in Example 41, wherein at least two of the amino acids have relative chirality. Example 46. A cyclic peptide as in any one of Examples 41 to 45, wherein at least two of the amino acids have the same chirality. Example 47. A cyclic peptide as in any one of Examples 41 to 46, wherein one arginine is adjacent to a hydrophobic amino acid. Example 48. A cyclic peptide as in Example 47, wherein the arginine has the same chirality as the adjacent hydrophobic amino acid. Example 49. A cyclic peptide as in any one of Examples 41 to 48, wherein at least two arginines are adjacent to each other. Example 50. A cyclic peptide as in any one of Examples 41 to 49, wherein three arginines are adjacent to each other. Example 51. A cyclic peptide as in any one of Examples 41 to 50, wherein at least two hydrophobic amino acids are adjacent to each other. Example 52. A cyclic peptide as in any one of Examples 41 to 51, wherein at least three hydrophobic amino acids are adjacent to each other. Example 53. A cyclic peptide as in any one of Examples 41 to 52, wherein any four adjacent amino acids are AA H2 -AA H1 -R-r, AA H2 -AA H1 -r-R, R-r-AA H1 -AA H2 、or r-R-AA H1 -AA H2 ,wherein AA H1 and AA H2Each of them is independently a hydrophobic amino acid. Example 54. A cyclic peptide according to any one of Examples 41 to 52, wherein the peptide has a structure according to any one of Formulas IV-A to IV-P: , , , , , , , , , , , , , , , , wherein: AA H1 and AA H2 Each of them is independently a hydrophobic amino acid. Example 55. A cyclic peptide according to Example 52 or 54, wherein AA H1 and AA H2 Each of them is independently piperidine-2-carboxylate, naphthylalanine, tryptophan, 3-(3-benzothienyl)-alanine, or phenylalanine, each of which is optionally substituted with one or more substituents. Example 56. A cyclic peptide according to any one of Examples 53 to 55, wherein AA H1 and AA H2 Each of them is independently a hydrophobic amino acid having a hydrophobicity greater than or equal to that of phenylalanine. Example 57. A cyclic peptide according to any one of Examples 53 to 56, wherein AA H1 is naphthylalanine. Example 58. A cyclic peptide according to any one of Examples 53 to 57, wherein AA H1 and AA H2 are naphthylalanine. Example 59. A cyclic peptide according to any one of Examples 53 to 57, wherein AA H1 is a hydrophobic amino acid having a large solvent-accessible surface area (SASA) in the side chain. Example 60. The cyclic peptide according to Example 59, wherein the large SASA is at least about 200 Å 2 . Example 61. A cyclic peptide according to any one of Examples 53 to 50, wherein when any AA U or any AA Z When it is a hydrophobic amino acid, the hydrophobic amino acid has a side chain with a SASA less than AA H1 The cyclic peptide according to any one of Examples 53 to 61, wherein the cyclic peptide does not include a hydrophobic amino acid with a SASA of the side chain greater than AA H1 The cyclic peptide according to any one of Examples 53 to 62, wherein AA H1 and AA H2 have the same or opposite chirality. Example 64. The cyclic peptide according to Example 63, wherein AA H1 and AA H2 have opposite chirality. Example 65. The cyclic peptide according to any one of Examples 53 to 64, wherein AA H1 has the same chirality as the adjacent arginine. Example 66. The cyclic peptide according to any one of Examples 53 to 65, which has one of the following sequences: AA H2 -AA H1 -R-r-R, AA H2 -AA H1 -R-r-r, AA H2 -AA H1 -r-R-R, AA H2 -AA H1 -r-R-r, R-R-r-AA H1 -AA H2 、r-R-r-AA H1 -AA H2 、r-r-R-AA H1 -AA H2 、or R-r-R-AA H1 -AA H2 。 Example 67. The cyclic peptides as in Examples 53 to 66 have one of the following sequences: AA H2 -LAA H1 -R-r-R, AA H2 -DAA H1 -r-R-r, r-R-r-DAA H1 -AA H2 、 or R-r-R-LAA H1 -AA H2 。 Example 68. A peptide comprising peptides of Formulae V-A to V-D: , , , or , wherein: AA H1 and AA H2 each of which is independently selected from hydrophobic amino acids; AA U and AA Z each occurrence is independently selected from amino acids, and each AA U and each AA Z at most one of which is arginine, and each of m and n is a number from 0 to 6, provided that at least one of m or n is not 0. Example 69. The peptide as in Example 68, wherein the amino group at the N-terminus or the carboxylate group at the C-terminus of any one of Formulae V-A to V-D independently forms a peptide bond. Example 70. The peptide as in Example 68, which further comprises a cyclized portion, wherein a cyclic peptide can be formed by the cyclized portion. Example 71. The peptide as in Example 70, wherein the cyclized portion independently forms a peptide bond with the amino group at the N-terminus or the carboxylate group at the C-terminus of any one of Formulae V-A to V-D. Example 72. The peptide as in any one of Examples 68 to 71, which further comprises a cargo portion (X n ), wherein at least one atom or bond is replaced by a bond connected to X n . Example 73. The cyclic peptide as in any one of Examples 68 to 72, wherein AA H1 and AA H2 each of which independently is a piperidine-2-carboxylate, naphthylalanine, tryptophan, 3-(3-benzothienyl)-alanine, or phenylalanine, each of which is optionally substituted with one or more substituents. Example 74. The cyclic peptide according to any one of Examples 68 to 73, wherein AA H1 and AA H2 each of which independently is a hydrophobic amino acid having a hydrophobicity greater than or equal to that of phenylalanine. Example 75. The cyclic peptide according to any one of Examples 68 to 74, wherein AA H1 is naphthylalanine. Example 76. The cyclic peptide according to any one of Examples 68 to 75, wherein AA H1 and AA H2 are naphthylalanine. Example 77. The cyclic peptide according to any one of Examples 68 to 76, wherein AA H1 is a hydrophobic amino acid having a large solvent-accessible surface area (SASA) in the side chain. Example 78. The cyclic peptide according to Example 77, wherein the large SASA is at least about 200 Å 2 . Example 79. The cyclic peptide according to any one of Examples 68 to 78, wherein AA H2 is a hydrophobic amino acid having a SASA of the side chain less than or equal to the SASA of the hydrophobic side chain of AA H1 . Example 80. The cyclic peptide according to any one of Examples 68 to 79, wherein when any AA U or any AA Z is a hydrophobic amino acid, the hydrophobic amino acid has a side chain with a SASA less than that of AA H1 . Example 81. The cyclic peptide according to any one of Examples 68 to 80, wherein AA H1 and AA H2 have the same or opposite chirality. Example 82. The cyclic peptide according to Example 81, wherein AA H1 and AA H2has relative chirality. Example 83. A cyclic peptide as in any one of Examples 68 to 82, wherein AA H1 has the same chirality as the adjacent arginine. Example 84. A cyclic peptide as in any one of Examples 68 to 83, having one of the following sequences: AA H2 -AA H1 -R-r-R, AA H2 -AA H1 -R-r-r, AA H2 -AA H1 -r-R-R, AA H2 -AA H1 -r-R-r, R-R-r-AA H1 -AA H2 , r-R-r-AA H1 -AA H2 , r-r-R-AA H1 -AA H2 , or R-r-R-AA H1 -AA H2 . Example 85. A cyclic peptide as in Examples 68 to 84, having one of the following sequences: AA H2 -LAA H1 -R-r-R, AA H2 -DAA H1 -r-R-r, r-R-r-DAA H1 -AA H2 , or R-r-R-LAA H1 -AA H2Example 86. A method for treating or diagnosing a patient in need thereof, comprising administering a cyclic peptide as in any one of Examples 41 to 67. Example 87. A composition comprising a cyclic peptide as in any one of Examples 41 to 67. Example 88. A peptide as in any one of Examples 68 to 85, wherein the cytosolic delivery efficiency of the peptide comprising any one of Formulas V-A to V-D is improved by an amount in the range of about 50% to about 500% compared to cyclo(FФRRRRQ) (SEQ ID NO:10). Example 89. The peptide of Example 88, wherein the peptide comprising any one of Formulas V-A to V-D comprises the following sequence: FfFRrR (SEQ ID NO:131). Example 90. The peptide of Example 88, wherein the peptide comprising any one of Formulas V-A to V-D comprises the following sequence: fFfrRr (SEQ ID NO:132). Example 91. The peptide of Example 88, wherein the peptide comprising any one of Formulas V-A to V-D comprises the following sequence: fFfRrR (SEQ ID NO:133). Example 92. The peptide of Example 88, wherein the peptide comprising any one of Formulas V-A to V-D comprises the following sequence: FfFrRr (SEQ ID NO:134). Example 93. The peptide of Example 88, wherein the peptide comprising any one of Formulas V-A to V-D comprises the following sequence: fFɸrRr (SEQ ID NO:135). Example 94. The peptide of Example 88, wherein the peptide comprising any one of Formulas V-A to V-D comprises the following sequence: fФfrRr (SEQ ID NO:136). Some embodiments of the invention have been described. However, it will be understood that various modifications can be made without departing from the spirit and scope of the invention. Accordingly, other embodiments are also within the scope of the following claims. Sequence Listing <![CDATA[<110> Ohio State Innovation Foundation]]> <![CDATA[<120> Cell Penetrating Peptide Sequences]]> <![CDATA[<130> 10336-333WO1]]> <![CDATA[<140> 106140322]]> <![CDATA[<141> 2017-11-21]]> <![CDATA[<150> US 62 / 425,550 ]]> <![CDATA[<151> 2016-11-12]]> <![CDATA[<150> US 62 / 425,438 ]]> <![CDATA[<151> 2016-11-12]]> <![CDATA[<150> US 62 / 438,141 ]]> <![CDATA[<151> 2016-12-22]]> <![CDATA[<150> US 62 / 507,483 ]]> <![CDATA[<151> 2017-05-17]]> <![CDATA[<160> 138 ]]> <![CDATA[<170> PatentIn version 3.5]]> <![CDATA[<210> 1]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<400> 1]]> Arg Arg Arg Arg Arg 1 5 <![CDATA[<210> 2]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<400> 2]]> Ala Ala Ala Ala Ala 1 5 <![CDATA[<210> 3]]> <![CDATA[<211> 4]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]] <![CDATA[<400> 3]]> Phe Phe Phe Phe 1 <![CDATA[<210> 4]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]] <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> Phosphocoumaryl alanine]] <![CDATA[<400> 4]]> Asp Glu Xaa Leu Ile 1 5 <![CDATA[<210> 5]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]] <![CDATA[<400> 5]]> Ala Ala Ala Ala Ala Ala Ala 1 5 <![CDATA[<210> 6]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<400> 6]]> Arg Ala Arg Ala Arg 1 5 <![CDATA[<210> 7]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<400> 7]]> Asp Ala Asp Ala Asp 1 5 <![CDATA[<210> 8]]> <![CDATA[<211> 4]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> Norleucine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> 2-Aminobutyric acid]]> <![CDATA[<400> 8]]> Asp Xaa Xaa Asp 1 <![CDATA[<210> 9]]> <![CDATA[<211> 4]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> misc_feature]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> Xaa can be any naturally occurring amino acid]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> 2-Aminobutyric acid]]> <![CDATA[<400> 9]]> Xaa Thr Arg Val 1 <![CDATA[<210> 10]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> SITE]]> <![CDATA[<222> (1]]>)..(5) <![CDATA[<223> Bonded at amino acid positions 1 and 5 to form a cyclic peptide]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> 2: L-2-Naphthylalanine]]> <![CDATA[<400> 10]]> Phe Xaa Arg Arg Arg Arg Gln 1 5 <![CDATA[<210> 11]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> L-Pipecolic acid]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<400> 11]]> Pro Xaa Gly Xaa Tyr 1 5 <![CDATA[<210> 12]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> L-Prolin]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(5)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<400> 12]]> Ser Xaa Ile Xaa Xaa 1 5 <![CDATA[<210> 13]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<400> 13]]> Ile His Ile Xaa Ile 1 5 <![CDATA[<210> 14]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222]]>> (2)..(2)]]> <![CDATA[<223> D-alanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(5)]]> <![CDATA[<223> L-proline]]> <![CDATA[<400> 14]]> <![CDATA[Ala Xaa Ile Xaa Xaa 1 5 <![CDATA[<210> 15]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> L-4-Fluorophenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> L-Pipecolic Acid]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(5)]]> <![CDATA[<223> D-Valine]]> <![CDATA[<400> 15]]> Xaa Ser Xaa Xaa Xaa 1 5 <![CDATA[<210> 16]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> L-Prolinic acid]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> D-Asparagine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<400> 16]]> Xaa Xaa Pro Xaa Ala 1 5 <![CDATA[<210> 17]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> L-Phenylglycine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<400> 17]]> Thr Xaa Ala Xaa Gly 1 5 <![CDATA[<210> 18]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(5)]]> <![CDATA[<223> D-Alanine]]> <![CDATA[<400> 18]]> Ala His Ile Xaa Xaa 1 5 <![CDATA[<210> 19]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> D-Asparagine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_R]]>ES <![CDATA[<222> (5)..(5)]]> <![CDATA[<223> D-Proline]]> <![CDATA[<400> 19]]> Gly Xaa Gly Xaa Xaa 1 5 <![CDATA[<210> 20]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> D-Phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> L-Prolinamine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<400> 20]]> Xaa Gln Xaa Xaa Ile 1 5 <![CDATA[<210> 21]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<400> 21]]> Ser Pro Gly Xaa His 1 5 <![CDATA[<210> 22]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> L-proline]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<400> 22]]> Xaa Tyr Ile Xaa His 1 5 <![CDATA[<210> 23]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> 2: D-valine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<400> 23]]> Ser Xaa Pro Xaa His 1 5 <![CDATA[<210> 24]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(5)]]> <![CDATA[<223> D-Asparagine]]> <![CDATA[<400> 24]]> Ala Ile Pro Xaa Xaa 1 5 <![CDATA[<210> 25]]> <![CDATA[<211> 6]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> L-4-Fluorophenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<400> 25]]> Xaa Ser Ile Xaa Gln Phe 1 5 <![CDATA[<210> 26]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> D-Alanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> L-Phenylglycine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(5)]]> <![CDATA[<223> D-Phenylalanine]]> <![CDATA[<400> 26]]> Ala Xaa Xaa Xaa Xaa 1 5 <![CDATA[<210> 27]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> D-Asparagine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> D-Threonine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> L-Phenylglycine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(5)]]> <![CDATA[<223> L-phenylglycine]]> <![CDATA[<400> 27]]> Xaa Xaa Xaa Xaa Xaa 1 5 <![CDATA[<210> 28]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> L-phenylglycine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(5)]]> <![CDATA[<223> L-norleucine]]> <![CDATA[<400> 28]]> Ile Pro Xaa Xaa Xaa 1 5 <![CDATA[<210> 29]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> L-Proline]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> L-4-Fluorophenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(5)]]> <![CDATA[<223> L-Proline]]> <![CDATA[<400> 29]]> Gln Xaa Xaa Xaa Xaa 1 5 <![CDATA[<210> 30]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> D-Asparagine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> L-4-Fluorophenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<400> 30]]> Xaa Ala Xaa Xaa Gly 1 5 <![CDATA[<210> 31]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> D-Amino acid]]> <![CDATA[<220>]]> <![CDATA[<221> misc_feature]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> Xaa can be any naturally occurring amino acid]]> <![CDATA[<220>]]> <![CDATA[<221> misc_feature]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> Xaa can be any naturally occurring amino acid]]> <![CDATA[<400> 31]]> Xaa Xaa Tyr Xaa Ala 1 5 <![CDATA[<210> 32]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> D-Glutamic acid]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> L-Phenylglycine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonodifluoromethyl)phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(5)]]> <![CDATA[<223> D-Valine]]> <![CDATA[<400> 32]]> Xaa Ala Xaa Xaa Xaa 1 5 <![CDATA[<210> 33]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> D-Valine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> L-Phenylglycine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonodifluoromethyl)phenylalanine]]> <![CDATA[<400> 33]]> Ile Xaa Xaa Xaa Ala 1 5 <![CDATA[<210> 34]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> D-Threonine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> L-Phenylglycine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<400> 34]]> Tyr Xaa Xaa Xaa Ala 1 5 <![CDATA[<210> 35]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> D-Asparagine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> L-Prolin]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> L-Phenylglycine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<400> 35]]> Xaa Xaa Xaa Xaa Ile 1 5 <![CDATA[<210> 36]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[ <222> (1)..(1)]]> <![CDATA[ <223> L-proline]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[ <222> (2)..(2)]]> <![CDATA[ <223> D-Aspartic Acid]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[ <222> (4)..(4)]]> <![CDATA[ <223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[ <400> 36]]> Xaa Xaa Trp Xaa His 1 5 <![CDATA[ <210> 37]]> <![CDATA[ <211> 5]]> <![CDATA[ <212> PRT]]> <![CDATA[ <213> Artificial Sequence]]> <![CDATA[ <220> ]]> <![CDATA[ <223> Synthetic Constructs]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[ <222> (2)..(2)]]> <![CDATA[ <223> L-proline]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[ <222> (3)..(3)]]> <![CDATA[ <223> D-Valamine]]> <![CDATA[ <220> ]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<400> 37]]> Tyr Xaa Xaa Xaa Ile 1 5 <![CDATA[<210> 38]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> D-Asparagine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<400> 38]]> Xaa Ser Ala Xaa Gly 1 5 <![CDATA[<210> 39]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> D-Threonine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> D-Asparagine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> D-Valine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(5)]]> <![CDATA[<223> D-Alanine]]> <![CDATA[<400> 39]]> Xaa Xaa Xaa Xaa Xaa 1 5 <![CDATA[<210> 40]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> D-Asparagine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> D-Threonine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> D-Valine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(5)]]> <![CDATA[<223> D-Threonine]]> <![CDATA[<400> 40]]> Xaa Xaa Xaa Xaa Xaa 1 5 <![CDATA[<210> 41]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> D-Threonine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonodifluoromethyl)phenylalanine]]> <![CDATA[<400> 41]]> Ser Ile Xaa Xaa Tyr 1 5 <![CDATA[<210> 42]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> D-Asparagine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[ <223> L-4-Fluorophenylalanine]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[ <222> (3)..(3)]]> <![CDATA[ <223> D-Aspartic Acid]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[ <222> (4)..(4)]]> <![CDATA[ <223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[ <222> (5)..(5)]]> <![CDATA[ <223> D-Leucine]]> <![CDATA[ <400> 42]]> Xaa Xaa Xaa Xaa Xaa 1 5 <![CDATA[ <210> 43]]> <![CDATA[ <211> 5]]> <![CDATA[ <212> PRT]]> <![CDATA[ <213> Artificial Sequence]]> <![CDATA[ <220> ]]> <![CDATA[ <223> Synthetic Constructs]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[ <222> (2)..(3)]]> <![CDATA[ <223> D-Aspartic Acid]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonodifluoromethyl)phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(5)]]> <![CDATA[<223> L-Norleucine]]> <![CDATA[<400> 43]]> Tyr Xaa Xaa Xaa Xaa 1 5 <![CDATA[<210> 44]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> D-Asparagine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> D-Asparagine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonodifluoromethyl)phenylalanine]]> <![CDATA[<400> 44]]> Xaa Tyr Xaa Xaa Gly 1 5 <![CDATA[<210> 45]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> D-Asparagine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<400>]]> 45 Ala Trp Xaa Xaa Ala 1 5 <![CDATA[<210> 46]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> D-Valine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> D-Threonine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<400> 46]]> Xaa Xaa His Xaa Tyr 1 5 <![CDATA[<210> 47]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> L-Phenylglycine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<22]]>2> (5)..(5)]]> <![CDATA[<223> L-proline]]> <![CDATA[<400> 47]]> <![CDATA[Pro Xaa His Xaa Xaa 1 5 <![CDATA[<210> 48]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> D-asparagine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> L-phenylglycine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<400> 48]]> Xaa Xaa His Xaa Gly 1 5 <![CDATA[<210> 49]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<400> 49]]> Pro Ala His Xaa Gly 1 5 <![CDATA[<210> 50]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<400> 50]]> Ala Tyr His Xaa Ile 1 5 <![CDATA[<210> 51]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> D-Asparagine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> L-Prolin]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> D-Glutamic acid]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonodifluoromethyl)phenylalanine]]> <![CDATA[<400> 51]]> Xaa Xaa Xaa Xaa Tyr 1 5 <![CDATA[<210> 52]]> <![CDATA[<211> 5]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> D-Valine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-4-(Phosphonyldifluoromethyl)phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(5)]]> <![CDATA[<223> D-Threonine]]> <![CDATA[<40]]>0> 52]]> <![CDATA[Xaa Ser Ser Xaa Xaa 1 5 <![CDATA[<210> 53]]> <![CDATA[<211> 8]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> D-Alanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> Sarcosine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> D-Threonine phosphate]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> L-Pipecolic acid]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(5)]]> <![CDATA[<223> L-β-Naphthylalanine]]> <![CDATA[<400> 53]]> Xaa Xaa Xaa Xaa Xaa Tyr Gln Lys 1 5 <![CDATA[<210> 54]]> <![CDATA[<211> 9]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> Trimesic acid]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> D-Alanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> Sarcosine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> D-Threonine phosphate]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(5)]]> <![CDATA[<223> L-Pipecolic acid]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (6)..(6)]]> <![CDATA[<223> L-β-Naphthylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (9)..(9)]]> <![CDATA[<223> L-2,3-Diaminopropionic acid]]> <![CDATA[<400> 54]]> Xaa Xaa Xaa Xaa Xaa Xaa Arg Ala Xaa 1 5 <![CDATA[<210> 55]]> <![CDATA[<211> 10]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> Trimesic acid]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> D-Alanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> Sarcosine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> D-Threonine phosphate]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(5)]]> <![CDATA[<223> L-Pipecolic acid]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[ <222> (6)..(6)]]> <![CDATA[ <223> L-β-Naphthylalanine]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[ <222> (9)..(9)]]> <![CDATA[ <223> D-Alanine]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD]]>_RES <![CDATA[ <222> (10)..(10)]]> <![CDATA[ <223> L-2,3-Diaminopropionic acid]]> <![CDATA[ <400> 55]]> Xaa Xaa Xaa Xaa Xaa Xaa Arg Ala Xaa Xaa 1 5 10 <![CDATA[ <210> 56]]> <![CDATA[ <211> 10]]> <![CDATA[ <212> PRT]]> <![CDATA[ <213> Artificial Sequence]]> <![CDATA[ <220> ]]> <![CDATA[ <223> Synthetic Constructs]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[ <222> (1)..(1)]]> <![CDATA[ <223> Trimesic acid]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> D-alanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> sarcosine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> D-threonine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(5)]]> <![CDATA[<223> L-pipecolic acid]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (6)..(6)]]> <![CDATA[<223> L-β-naphthylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (9)..(9)]]> <![CDATA[<223> D-alanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (10)..(10)]]> <![CDATA[<223> L-2,3-diaminopropionic acid]]> <![CDATA[<400> 56]]> Xaa Xaa Xaa Xaa Xaa Xaa Arg Ala Xaa Xaa 1 5 10 <![CDATA[<210> 57]]> <![CDATA[<211> 10]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> Trimesic Acid]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> D-Alanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> Sarcosine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> D-Threonine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(5)]]> <![CDATA[ <223> D-Alanine]]> <![CDATA[ <220> ]]> <![CDATA[<22]]> 1> MOD_RES]]> <![CDATA[ <222> (6)..(6)]]> <![CDATA[ <223> L-β-Naphthylalanine]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[ <222> (9)..(9)]]> <![CDATA[ <223> D-Alanine]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[ <222> (10)..(10)]]> <![CDATA[ <223> L-2,3-Diaminopropionic acid]]> <![CDATA[ <400> 57]]> <![CDATA[Xaa Xaa Xaa Xaa Xaa Xaa Arg Ala Xaa Xaa 1 5 10 <![CDATA[ <210> 58]]> <![CDATA[ <211> 6]]> <![CDATA[ <212> PRT]]> <![CDATA[ <213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> SITE]]> <![CDATA[<222> (1)..(6)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 6 to form a cyclic peptide]]> <![CDATA[<400> 58]]> Phe Phe Arg Arg Arg Gln 1 5 <![CDATA[<210> 59]]> <![CDATA[<211> 6]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> SITE]]> <![CDATA[<222> (1)..(6)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 6 to form a cyclic peptide]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> D-arginine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(5)]]> <![CDATA[<223> D-arginine]]> <![CDATA[<400> 59]]> Phe Phe Xaa Arg Xaa Gln 1 5 <![CDATA[<210> 60]]> <![CDATA[<211> 6]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> SITE]]> <![CDATA[<222> (1)..(6)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 6 to form a cyclic peptide]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> D-arginine]]> <![CDATA[<400> 60]]> Phe Phe Arg Xaa Arg Gln 1 5 <![CDATA[<210> 61]]> <![CDATA[<211> 6]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(6)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 6 to form a cyclic peptide]]> <![CDATA[<400> 61]]> Phe Arg Phe Arg Arg Gln 1 5 <![CDATA[<210> 62]]> <![CDATA[<211> 6]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(6)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 6 to form a cyclic peptide]]> <![CDATA[<400> 62]]> Phe Arg Arg Phe Arg Gln 1 5 <![CDATA[<210> 63]]> <![CDATA[<211> 6]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(6)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 6 to form a cyclic peptide]]> <![CDATA[<400> 63]]> Phe Arg Arg Arg Phe Gln 1 5 <![CDATA[<210> 64]]> <![CDATA[<211> 6]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(6)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 6 to form a cyclic peptide]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> L-2-Naphthylalanine]]> <![CDATA[<400> 64]]> Gly Xaa Arg Arg Arg Gln 1 5 <![CDATA[<210> 65]]> <![CDATA[<211> 6]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(6)]]> <![CDATA[<223> Bonding at amino acid positions 1 and 6 to form a cyclic peptide]]> <![CDATA[<400> 65]]> Phe Phe Phe Arg Ala Gln 1 5 <![CDATA[<210> 66]]> <![CDATA[<211> 6]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(6)]]> <![CDATA[<223> Bonding at amino acid positions 1 and 6 to form a cyclic peptide]]> <![CDATA[<400> 66]]> Phe Phe Phe Arg Arg Gln 1 5 <![CDATA[<210> 67]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonding at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<400> 67]]> Phe Phe Arg Arg Arg Arg Gln 1 5 <![CDATA[<210> 68]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<400> 68]]> Phe Arg Arg Phe Arg Arg Gln 1 5 <![CDATA[<210> 69]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<400> 69]]> Phe Arg Arg Arg Phe Arg Gln 1 5 <![CDATA[<210> 70]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<400> 70]]> Arg Phe Phe Arg Arg Arg Gln 1 5 <![CDATA[<210> 71]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<400> 71]]> Arg Phe Arg Arg Phe Arg Gln 1 5 <![CDATA[<210> 72]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<400> 72]]> Phe Arg Phe Arg Arg Arg Gln 1 5 <![CDATA[<210> 73]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> ]]> (1)..(7) <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<400> 73]]> Phe Phe Phe Arg Arg Arg Gln 1 5 <![CDATA[<210> 74]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<400> 74]]> Phe Phe Arg Arg Arg Phe Gln 1 5 <![CDATA[<210> 75]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<400> 75]]> Phe Arg Phe Phe Arg Arg Gln 1 5 <![CDATA[<210> 76]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<400> 76]]> Arg Arg Phe Phe Phe Arg Gln 1 5 <![CDATA[<210> 77]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<400> 77]]> Phe Phe Arg Phe Arg Arg Gln 1 5 <![CDATA[<210> 78]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220]]>>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<400> 78]]> <![CDATA[Phe Phe Arg Arg Phe Arg Gln 1 5 <![CDATA[<210> 79]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> ]]> Synthetic construct <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<400> 79]]> Phe Arg Arg Phe Phe Arg Gln 1 5 <![CDATA[<210> 80]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Linking at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<400> 80]]> Phe Arg Arg Phe Arg Phe Gln 1 5 <![CDATA[<210> 81]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> ]]> Synthetic construct <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Linking at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<400> 81]]> Phe Arg Phe Arg Phe Arg Gln 1 5 <![CDATA[<210> 82]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial]] sequence <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonding at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<400> 82]]> Arg Phe Phe Arg Phe Arg Gln 1 5 <![CDATA[<210> 83]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonding at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> L-2-Naphthylalanine]]> <![CDATA[<400> 83]]> Gly Xaa Arg Arg Arg Arg Gln 1 5 <![CDATA[<210> 84]]> <![CDATA[<211> 8]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(8)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 8 to form a cyclic peptide]]> <![CDATA[<400> 84]]> Phe Phe Phe Arg Arg Arg Arg Gln 1 5 <![CDATA[<210> 85]]> <![CDATA[<211> 8]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(8)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 8 to form a cyclic peptide]]> <![CDATA[<400> 85]]> Arg Phe Phe Arg Arg Arg Arg Gln 1 5 <![CDATA[<210> 86]]> <![CDATA[<211> 8]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(8)]]> <![CDATA[<223> Bond between amino acid positions 1 and 8 to form a cyclic peptide]]> <![CDATA[<400> 86]]> Arg Arg Phe Phe Arg Arg Arg Gln 1 5 <![CDATA[<210> 87]]> <![CDATA[<211> 8]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(8)]]> <![CDATA[<223> Bond between amino acid positions 1 and 8 to form a cyclic peptide]]> <![CDATA[<400> 87]]> Arg Phe Phe Phe Arg Arg Arg Gln 1 5 <![CDATA[<210> 88]]> <![CDATA[<211> 8]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(8)]]> <![CDATA[<223> Bond between amino acid positions 1 and 8 to form a cyclic peptide]]> <![CDATA[<400> 88]]> Arg Arg Phe Phe Phe Arg Arg Gln 1 5 <![CDATA[<210> 89]]> <![CDATA[<211> 8]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(8)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 8 to form a cyclic peptide]]> <![CDATA[<400> 89]]> Phe Phe Arg Arg Phe Arg Arg Gln 1 5 <![CDATA[<210> 90]]> <![CDATA[<211> 8]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(8)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 8 to form a cyclic peptide]]> <![CDATA[<400> 90]]> Phe Phe Arg Arg Arg Arg Phe Gln 1 5 <![CDATA[<210> 91]]> <![CDATA[<211> 8]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(8)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 8 to form a cyclic peptide]]> <![CDATA[<400> 91]]> Phe Arg Arg Phe Phe Arg Arg Gln 1 5 <![CDATA[<210> 92]]> <![CDATA[<211> 9]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(9)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 9 to form a cyclic peptide]]> <![CDATA[<400> 92]]> Phe Phe Phe Arg Arg Arg Arg Arg Gln 1 5 <![CDATA[<210> 93]]> <![CDATA[<211> 10]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(10)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 10 to form a cyclic peptide]]> <![CDATA[<400> 93]]> Phe Phe Phe Arg Arg Arg Arg Arg Arg Gln 1 5 10 <![CDATA[<210> 94]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<220>]]> <![CDATA[<221> mod_res]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> L-2-Naphthylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> mod_res]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> D-arginine]]> <![CDATA[<220>]]> <![CDATA[<221> mod_res]]> <![CDATA[<222> (6)..(6)]]> <![CDATA[<223> D-arginine]]> <![CDATA[<400> 94]]> Phe Xaa Arg Xaa Arg Xaa Gln 1 5 <![CDATA[<210> 95]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(2)]]> <![CDATA[<223> L-4-fluorophenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<400> 95]]> Xaa Xaa Arg Arg Arg Arg Gln 1 5 <![CDATA[<210> 96]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> D-Phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(5)]]> <![CDATA[<223> D-Arginine]]> <![CDATA[<400> 96]]> Phe Xaa Phe Arg Xaa Arg Gln 1 5 <![CDATA[<210> 97]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> D-Phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> D-Phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MO]]>D_RES <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> D-Arginine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (6)..(6)]]> <![CDATA[<223> D-Arginine]]> <![CDATA[<400> 97]]> Xaa Phe Xaa Xaa Arg Xaa Gln 1 5 <![CDATA[<210> 98]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> D-Phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> D-Phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(5)]]> <![CDATA[<223> D-Arginine]]> <![CDATA[<400> 98]]> Xaa Phe Xaa Arg Xaa Arg Gln 1 5 <![CDATA[<210> 99]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[ <222> (2)..(2)]]> <![CDATA[ <223> D-Phenylalanine]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[ <222> (4)..(4)]]> <![CDATA[ <223> D-Arginine]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[ <222> (6)..(6)]]> <![CDATA[ <223> D-Arginine]]> <![CDATA[ <400> 99]]> Phe Xaa Phe Xaa Arg Xaa Gln 1 5 <![CDATA[ <210> 100]]> <![CDATA[ <211> 7]]> <![CDATA[ <212> PRT]]> <![CDATA[ <213> Artificial Sequence]]> <![CDATA[ <220> ]]> <![CDATA[ <223> Synthetic Constructs]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[ <222> (1)..(1)]]> <![CDATA[ <223> D-Phenylalanine]]> <![CDATA[ <220> ]]> <![CDATA[ <221> site]]> <![CDATA[ <222> (1)..(7)]]> <![CDATA[<223> Bonding at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> D-2-Naphthylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> D-Arginine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (6)..(6)]]> <![CDATA[<223> D-Arginine]]> <![CDATA[<400> 100]]> Xaa Phe Xaa Xaa Arg Xaa Gln 1 5 <![CDATA[<210> 101]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> D-Phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> L-2-Naphthylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> D-Phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> D-Arginine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (6)..(6)]]> <![CDATA[<223> D-Arginine]]> <![CDATA[<400> 101]]> Xaa Xaa Xaa Xaa Arg Xaa Gln 1 5 <![CDATA[<210> 102]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> D-2-Naphthylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> D-Phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (4)..(4)]]> <![CDATA[<223> D-Arginine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (6)..(6)]]> <![CDATA[<223> D-Arginine]]> <![CDATA[<400> 102]]> Xaa Phe Xaa Xaa Arg Xaa Gln 1 5 <![CDATA[<210> 103]]> <![CDATA[<211> 6]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(6)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 6 to form a cyclic peptide]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> L-2-Naphthylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> D-Arginine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(5)]]> <![CDATA[<223> D-Arginine]]> <![CDATA[<400> 103]]> Phe Xaa Xaa Arg Xaa Gln 1 5 <![CDATA[<210> 104]]> <![CDATA[<211> 6]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> D-Phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(6)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 6 to form a cyclic peptide]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> L-2-Naphthylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> D-Arginine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(5)]]> <![CDATA[<223> D-arginine]]> <![CDATA[<400> 104]]> <![CDATA[Xaa Xaa Xaa Arg Xaa Gln 1 5 <![CDATA[<210> 105]]> <![CDATA[<211> 8]]> <![CDATA[<212> PRT]]> <![CDATA[<213> artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> ACETYLATION]]> <![CDATA[<220>]]> <![CDATA[<221> misc_feature]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> Xaa can be any naturally occurring amino acid]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> D-Phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> misc_feature]]> <![CDATA[<222> (5).]]>.(5) <![CDATA[<223> Xaa can be any naturally occurring amino acid]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (6)..(6)]]> <![CDATA[<223> D-Arginine]]> <![CDATA[<220>]]> <![CDATA[<221> misc_feature]]> <![CDATA[<222> (7)..(7)]]> <![CDATA[<223> Xaa can be any naturally occurring amino acid]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (8)..(8)]]> <![CDATA[<223> D-Arginine]]> <![CDATA[<400> 105]]> Lys Xaa Phe Arg Xaa Arg Xaa Asp 1 5 <![CDATA[<210> 106]]> <![CDATA[<211> 8]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[ <222> (1)..(1)]]> <![CDATA[ <223> ACETYLATION]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[ <222> (1)..(1)]]> <![CDATA[ <223> L-2,3-Diaminopropionic acid]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[ <222> (2)..(2)]]> <![CDATA[ <223> D-Phenylalanine]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[ <222> (5)..(5)]]> <![CDATA[ <223> D-Arginine]]> <![CDATA[ <220> ]]> <![CDATA[ <221> MOD_RES]]> <![CDATA[ <222> (7)..(7)]]> <![CDATA[ <223> D-Arginine]]> <![CDATA[ <400> 106]]> Xaa Xaa Phe Arg Xaa Arg Xaa Asp 1 5 <![CDATA[ <210> 107]]> <![CDATA[ <211> 8]]> <![CDATA[ <212> PRT]]> <![CDATA[ <213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<400> 107]]> Cys Trp Trp Arg Arg Arg Arg Cys 1 5 <![CDATA[<210> 108]]> <![CDATA[<211> 9]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<400> 108]]> Cys Trp Trp Val Arg Arg Arg Arg Cys 1 5 <![CDATA[<210> 109]]> <![CDATA[<211> 8]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<400> 109]]> Cys Phe Trp Arg Arg Arg Arg Cys 1 5 <![CDATA[<210> 110]]> <![CDATA[<211> 8]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<400> 110]]> Cys Trp Trp Trp Arg Arg Arg Cys 1 5 <![CDATA[<210> 111]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> Pyrrolysine]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> Naphthylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(6)]]> <![CDATA[<223> D-Arginine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (7)..(7)]]> <![CDATA[<223> D-Glutamic acid]]> <![CDATA[<400> 111]]> Xaa Xaa Arg Glu Xaa Xaa Xaa 1 5 <![CDATA[<210> 112]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> Pyrrolysine]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223>]]> Bonded at amino acid positions 1 and 7 to form a cyclic peptide <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> Naphthylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(6)]]> <![CDATA[<223> D-Arginine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (7)..(7)]]> <![CDATA[<223> D-Glutamic acid]]> <![CDATA[<400> 112]]> Xaa Xaa Arg Arg Xaa Xaa Xaa 1 5 <![CDATA[<210> 113]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> Pyrrolysine]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(3)]]> <![CDATA[<223> Naphthylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(6)]]> <![CDATA[<223> D-Arginine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (7)..(7)]]> <![CDATA[<223> D-Glutamic acid]]> <![CDATA[<400> 113]]> Xaa Xaa Xaa Arg Xaa Xaa Xaa 1 5 <![CDATA[<210> 114]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> L-Prolin]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(3)]]> <![CDATA[<223> Naphthylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(6)]]> <![CDATA[<223> D-arginine]]> <![CDATA[<400> 114]]> Xaa Xaa Xaa Arg Xaa Xaa Glu 1 5 <![CDATA[<210> 115]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic Construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> L-proline]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> Naphthylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(6)]]> <![CDATA[<223> D-arginine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (7)..(7)]]> <![CDATA[<223> D-Glutamic acid]]> <![CDATA[<400> 115]]> Xaa Xaa Phe Arg Xaa Xaa Xaa 1 5 <![CDATA[<210> 116]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> Pyrrolysine]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> Naphthylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(6)]]> <![CDATA[<223> D-Arginine]]> <![CDATA[<400> 116]]> Xaa Xaa Phe Arg Xaa Xaa Glu 1 5 <![CDATA[<210> 117]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> Pyrrolysine]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> Naphthylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> D-Phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(6)]]> <![CDATA[<223> D-arginine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (7)..(7)]]> <![CDATA[<223> D-glutamic acid]]> <![CDATA[<400> 117]]> Xaa Xaa Xaa Arg Xaa Xaa Xaa 1 5 <![CDATA[<210> 118]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> artificial sequence]]> <![CDATA[<220>]]> <![CDATA[<223> synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> cis-proline]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(2)]]> <![CDATA[<223> naphthylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (3)..(3)]]> <![CDATA[<223> D-Phenylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(6)]]> <![CDATA[<223> D-Arginine]]> <![CDATA[<400> 118]]> Xaa Xaa Xaa Arg Xaa Xaa Glu 1 5 <![CDATA[<210> 119]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223>]]> Synthetic Construct <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (1)..(1)]]> <![CDATA[<223> L-Proline]]> <![CDATA[<220>]]> <![CDATA[<221> site]]> <![CDATA[<222> (1)..(7)]]> <![CDATA[<223> Bonded at amino acid positions 1 and 7 to form a cyclic peptide]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (2)..(3)]]> <![CDATA[<223> Naphthylalanine]]> <![CDATA[<220>]]> <![CDATA[<221> MOD_RES]]> <![CDATA[<222> (5)..(6)]]> <![CDATA[<223> D-arginine]]> <![CDATA[<400> 119]]> Xaa Xaa Xaa Arg Xaa Xaa Glu 1 5 <![CDATA[<210> 120]]> <![CDATA[<211> 7]]> <![CDATA[<212> PRT]]> <![CDATA[<213> Artificial Sequence]]> <![CDATA[<220>]]> <![CDATA[<223> Synthetic construct]]> <![CDATA[<220>]]> <![CDATA[<221> MISC_FEATURE]]> <![CDATA[<222&...

Claims

1. A cyclic peptide comprising the following sequences: cyclic (FFFRRRQ) (SEQ ID NO:73); cyclic (RRFFFRQ) (SEQ ID NO:76); cyclic (RFFFRRRQ) (SEQ ID NO:87); cyclic (FFRRRRFQ) (SEQ ID NO:90); cyclic (FΦRrRrQ) (SEQ ID NO:94); cyclic (XXRRRRQ) (SEQ ID NO:95); cyclic (FfFRrQ) (SEQ ID NO:96); cyclic (fFfrRrQ) (SEQ ID NO:97); cyclic (fFfRrRQ) (SEQ ID NO:98); cyclic (FfFrRrQ) (SEQ ID NO:99); cyclic (fFɸrRrQ) (SEQ ID NO:100); or cyclic (fФfrRrQ) (SEQ ID NO:101); Cyclic (fΦrRrQ) (SEQ ID NO:104); Cyclic (Pip-Nal-Nal-Arg-arg-arg-glu) (SEQ ID NO:113); Cyclic (Pip-Nal-Nal-Arg-arg-arg-Glu) (SEQ ID NO:114); or Cyclic (Pip-Nal-nal-Arg-arg-arg-Glu) (SEQ ID NO:119) wherein F is L-phenylalanine, f is D-phenylalanine, R and Arg are L-arginine, r and arg are D-arginine, Q and Glu are L-glutamic acid, glu is D-glutamic acid, X is L-4-fluorophenylalanine, Pip is L-proline, ɸ and nal are D-naphthylalanine, and Ф and Nal are L-naphthylalanine.

2. The cyclic peptide of claim 1, wherein at least one bond in the cyclic peptide is replaced by a bond linked to a cargo portion Xn.

3. The cyclic peptide of claim 1, wherein a cargo portion Xn is coupled to a side chain of an amino acid in the cyclic peptide.

4. The cyclic peptide of claim 2 or 3, wherein the cargo portion comprises one or more detectable portions, one or more therapeutic portions, one or more targeted portions, or any combination thereof.

5. The cyclic peptide of claim 4, wherein the cargo portion comprises a therapeutic portion.

6. The cyclic peptide of claim 5, wherein the therapeutic portion comprises an anticancer agent, an antiviral agent, an antimicrobial agent, an anti-inflammatory agent, an immunosuppressant, an anesthetic, or any combination thereof.

7. A pharmaceutical composition comprising a cyclic peptide as claimed in any one of claims 1 to 6 and a pharmaceutically acceptable carrier.

8. The pharmaceutical composition of claim 7, wherein the pharmaceutical composition is formulated for non-enteral administration.