Claims
- 1. A sol-gel system comprising a peptide amphiphile compound having a bioactive epitope sequence, a hydrophobic component, and a net charge at substantially physiological pH; and a reagent to induce gelation of said amphiphile compound.
- 2. The system of claim 1 wherein said reagent comprises a metal ion and said system is a gel of supramolecular nanofibers of said amphiphile compound.
- 3. The system of claim 2 wherein said ion is selected from the group consisting of Ca, Mg, Cd, Fe and Zn divalent ions, Al, Fe and Gd trivalent ions, and combinations of said ions.
- 4. The system of claim 3 wherein said metal ion is in stoichiometric excess of said amphiphile compound.
- 5. The system of claim 1 wherein said peptide component of said amphiphile compound comprises a residue with a functional moiety capable of intermolecular covalent bond formation.
- 6. The system of claim 5 wherein said residue is cysteine.
- 7. The system of claim 6 further comprising an oxidizing agent to form a disulfide bond between amphiphile compounds.
- 8. The system of claim 7 further comprising a subsequent reducing agent to cleave said disulfide bond.
- 9. The system of claim 1 wherein said peptide amphiphile compound has a net charge, and said reagent comprises an aqueous solution of another peptide amphiphile compound with an opposite net charge at substantially physiological pH, and said system is a network of nanofibers of said amphiphile compounds.
- 10. The system of claim 9 wherein said peptide components of said amphiphile compounds comprise a residue with a functional moiety capable of intermolecular covalent bond formation.
- 11. The system of claim 10 wherein said residue is cysteine.
- 12. The system of claim 11 further comprising an oxidizing agent to form a disulfide bond between amphiphile compounds.
- 13. The system of claim 12 further comprising a subsequent reducing agent to cleave said disulfide bond.
- 14. The system of claim 1 wherein said bioactive epitope sequence is selected from RGD, IKVAV and YIGSR.
- 15. The system of claim 1 wherein said peptide amphiphile compound has a net positive charge, and said reagent provides said system a basic pH, and said system comprises a network of nanofibers of said amphiphile compounds.
- 16. The system of claim 15 wherein said reagent comprises hydroxide ion.
- 17. A method of peptide amphiphile nanofiber formation, said method comprising:
providing an aqueous medium including a peptide amphiphile compound having a peptide component with a bioactive epitope sequence, and a hydrophobic component, said hydrophobic component sufficient to afford nanofiber formation of said compound; placing said medium on a surface; and removing said aqueous component from said medium.
- 18. The method of claim 17 wherein said removal is passive drying.
- 19. The method of claim 17 wherein said amphiphile compound has a net charge at a physiological pH.
- 20. The method of claim 17 wherein said bioactive sequence is RGD.
- 21. The composition of claim 14 wherein said bioactive sequence is IKVAV.
- 22. The method of claim 17 wherein said peptide component further comprises at least one phosphorylated residue.
- 23. The method of claim 17 wherein said hydrophobic component comprises an alkyl moiety of at least six carbon units.
- 24. A method of peptide amphiphile nanofiber formation, said method comprising:
providing an aqueous medium comprising a peptide amphiphile compound having a bioactive epitope sequence, a hydrophobic component, and a net charge at substantially physiological pH; and introducing a reagent to said medium to induce nanofiber formation.
- 25. The method of claim 24 wherein said reagent comprises a metal ion.
- 26. The method of claim 24 wherein said peptide amphiphile compound has a net charge, and said reagent comprises an aqueous medium of another peptide amphiphile compound with an opposite net charge at substantially physiological pH.
- 27. The method of claim 24 wherein said peptide amphiphile compound has a net positive charge and said reagent provides said medium a basic pH.
- 28. A peptide amphiphile composition comprising a first peptide component comprising a hydrophobic moiety and a first amino acid sequence, said sequence further comprising a first bioactive epitope sequence; and a second peptide component comprising a hydrophobic moiety and a second amino acid sequence, said sequence further comprising a second bioactive epitope sequence, said first amino acid sequence having a net charge at a physiological pH, and said second amino acid sequence having a net charge at a physiological pH opposite said net charge of said first amino acid sequence.
- 29. The composition of claim 28 wherein each of said first and second bioactive epitope sequences is selected from RGD, IKVAV and YIGSR.
- 30. The composition of claim 28 wherein each of said first and second peptide components comprise a residue with a functional moiety capable of intermolecular covalent bond formation.
- 31. The composition of claim 30 wherein said residue is cysteine.
- 32. The composition of claim 28 wherein at least one of said first and second peptide components further comprises at least one phosphorylated residue.
- 33. The composition of claim 28 having a nanofibrous structured assembly.
Parent Case Info
[0001] This application claims priority benefit from U.S. provisional application Ser. No. 60/357,228 filed Feb. 15, 2002, the entirety of which is incorporated herein by reference.
Government Interests
[0002] The United States government has certain rights to this invention pursuant to Grant Nos. DE-FG02-00ER45810/A001, DMR-9996253 and F49620-00-1-0283/P01 from, respectively, the DOE, NSF and AFOSR-MURI to Northwestern University.
Provisional Applications (1)
|
Number |
Date |
Country |
|
60357228 |
Feb 2002 |
US |