Peptide-amphiphile nanofibers: a versatile scaffold for the preparation of self-assembling materials.
Twelve derivatives of peptide-amphiphile molecules, designed to self-assemble into nanofibers, are described. The scope of amino acid selection and alkyl tail modification in the peptide-amphiphile molecules are investigated, yielding nanofibers varying in morphology, surface chemistry, and potential bioactivity. The results demonstrate the chemically versatile nature of this supramolecular system and its high potential for manufacturing nanomaterials. In addition, three different modes of self-assembly resulting in nanofibers are described, including pH control, divalent ion induction, and concentration.
Hartgerink
Jeffrey D
JD
Department of Chemistry and Materials Science, Medical School, Northwestern University, Evanston, IL 60208, USA.
Beniash
Elia
E
Stupp
Samuel I
SI
D000596:Amino Acids / Q000737:chemistry; D002621:Chemistry / Q000379:methods*; D003432:Cross-Linking Reagents / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007477:Ions; D008854:Microscopy, Electron; D008956:Models, Chemical; D008958:Models, Molecular; D036103:Nanotechnology; D010100:Oxygen / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D010772:Phosphotungstic Acid / Q000737:chemistry; D017434:Protein Structure, Tertiary
D000596:Amino Acids; D003432:Cross-Linking Reagents; D007477:Ions; D010455:Peptides; D010772:Phosphotungstic Acid; D010100:Oxygen