# US 7,745,708 B2 · Self-assembly of peptide-amphiphile nanofibers under physiological conditions > Agents: this data is available as JSON from the patentgrep API and MCP server — see https://patentgrep.com/llms.txt - Number: US 7,745,708 B2 - Document ID: US7745708B2 - Status: Granted - Kind: B2 - Application number: 11/863,975 - Filed: 2007-09-28 - Published: 2008-07-24 - Granted: 2010-06-29 - Earliest claimed: 2002-02-15 - Assignees: Northwestern University - Inventors: Samuel I. Stupp; Jeffrey D. Hartgerink; Elia Beniash - Web page: https://patentgrep.com/patent/US7745708B2 ## CPC - C07K 14/78: Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin or cold insoluble globulin [CIG] - A61K 38/00: Medicinal preparations containing peptides (peptides containing beta-lactam rings A61K31/00; cyclic dipeptides not having in their molecule any other peptide link than those which form their ring, e.g. piperazine-2,5-diones, A61K31/00; ergot alkaloids of the cyclic peptide type A61K31/48; containing macromolecular compounds having statistically distributed amino acid units A61K31/74; medicinal preparations containing antigens or antibodies A61K39/00; medicinal preparations characterised by the non-active ingredients, e.g. peptides as drug carriers, A61K47/00) - Y10S 977/705: Protein or peptide - Y10T 428/12014: having metal particles - Y10T 428/24413: Metal or metal compound - C07K: PEPTIDES (peptides in foodstuffs A23; obtaining protein compositions for foodstuffs, working-up proteins for foodstuffs A23J; preparations for medicinal purposes A61K; peptides containing beta-lactam rings C07D; cyclic dipeptides not having in their molecule any other peptide link than those which form their ring, e.g. piperazine-2,5-diones, C07D; ergot alkaloids of the cyclic peptide type C07D519/02; macromolecular compounds having statistically distributed amino acid units in their molecules, i.e. when the preparation does not provide for a specific; but for a random sequence of the amino acid units, homopolyamides and block copolyamides derived from amino acids C08G69/00; macromolecular products derived from proteins C08H1/00; preparation of glue or gelatine C09H; single cell proteins, enzymes C12N; genetic engineering processes for obtaining peptides C12N15/00; compositions for measuring or testing processes involving enzymes C12Q; investigation or analysis of biological material G01N33/00) - A61K: PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES (devices or methods specially adapted for bringing pharmaceutical products into particular physical or administering forms A61J3/00; chemical aspects of, or use of materials for deodorisation of air, for disinfection or sterilisation, or for bandages, dressings, absorbent pads or surgical articles A61L; soap compositions C11D) - Y10S: TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS - Y10T: TECHNICAL SUBJECTS COVERED BY FORMER US CLASSIFICATION ## Abstract Peptide amphiphile compounds, compositions and methods for self-assembly or nanofibrous network formation under neutral or physiological conditions. ## Claims ### Claim 1 A method of making a cylindrical micellar nanofiber composed of beta-sheets of peptide segment of peptide amphiphile comprising the steps of: (a) providing the peptide amphiphile molecule in an aqueous solution, wherein said peptide amphiphile molecule comprises a single C6 to C22 linear hydrocarbon segment covalently linked to a peptide segment comprising a bioactive epitope sequence selected from RGD, KGE, IKVAV (SEQ ID NO: 1) and YIGSR (SEQ ID NO: 20); and (b) contacting said peptide amphiphile molecule with an effective amount of a metal ion sufficient to induce formation of a cylindrical micellar nanofiber composed of beta-sheets. ### Claim 2 (depends on 1) The method of claim 1, wherein said contacting step occurs under physiological conditions. ### Claim 3 (depends on 1) The method of claim 1, wherein said metal ion is present in a bodily fluid. ### Claim 4 (depends on 1) The method of claim 1, wherein the metal ion selected from the group consisting of Ca2+, Mg2+, Cd2+, Fe2+ and Zn2+ divalent ions, Al3+, Fe3+, and Gd3+ trivalent ions, and combination of said ions. ### Claim 5 (depends on 1) The method of claim 1, wherein said peptide amphiphile molecule has a net charge at substantially physiological pH. ### Claim 6 (depends on 1) The method of claim 1, wherein said peptide segment further comprises at least one phosphorylated residue. ### Claim 7 (depends on 6) The method of claim 6, wherein said phosphorylated residue is phosphoserine. ### Claim 8 (depends on 1) The method of claim 1, wherein said peptide segment further comprises a residue with a functional moiety capable of intermolecular covalent bond formation. ### Claim 9 (depends on 8) The method of claim 8, wherein said residue is cysteine. ### Claim 10 (depends on 9) The method of claim 9, wherein said peptide segment further comprises at least one phosphoserine residue. ### Claim 11 (depends on 10) The method of claim 10, wherein said peptide segment further comprises at least one glycine residue between said cysteine and phosphoserine residues. ### Claim 12 (depends on 1) The method of claim 1, wherein said peptide segment comprises a first peptide sequence selected from the group consisting of CCCCGGGS(p) (SEQ ID NO: 3), CCCCGGGS (SEQ ID NO: 26), CCCCGGGE (SEQ ID NO: 27), AAAAGGGS(p) (SEQ ID NO: 28), AAAAGGGS (SEQ ID NO: 29), GGGS(p) (SEQ ID NO: 30), and GGGS (SEQ ID NO: 31) and a second peptide sequence selected from RGD, KGE, IKVAV (SEQ ID NO: 1) and YIGSR (SEQ ID NO: 20), wherein S(p) stands for phosphorylated serine residue. ### Claim 13 (depends on 1) The method of claim 1, wherein said hydrocarbon segment is linked to the N-terminus of said peptide segment. ### Claim 14 (depends on 1) The method of claim 1, wherein said cylindrical micellar nanofiber has dimensional and functional characteristics mimetic of collagen fibrils. ### Claim 15 (depends on 1) The method of claim 1, wherein said cylindrical micellar nanofiber forms a conical shape comprised of a narrow hydrocarbon tail at one end and a bulkier peptide region at the other. ### Claim 16 (depends on 1) The method of claim 1, wherein said cylindrical micellar nanofiber displays a secondary structure that includes both beta-sheets and alpha-helices.