Proceedings of the National Academy of Sciences · 2002 · 1.2K citations · 40 references
Amino Acid SelectionNanomedicineBiofunctional MaterialNanofiberEngineeringPeptide-amphiphile NanofibersSelf-assemblyPeptide EngineeringPolymer Self-assemblyBiofabricationTwelve DerivativesVersatile ScaffoldAmphiphilic SystemBiomedical EngineeringMolecular EngineeringSelf-assembling MaterialsSupramolecular SystemBiomolecular Engineering
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.
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Principles that Govern the Folding of Protein Chains
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