Abstract
Abstract An amphiphilic peptide designed with serine as a polar residue showed gelation in both water and organic solvents. This sequential peptide has a strong tendency to adopt β-sheet conformation in these solvents. Such gels of β-sheet peptide based on hierarchical self-assembly consist of nanofiber construction because of the β-sheet structure, and because of crosslinking attributable to hydrogen bonding among hydroxy groups of the serine side chain.
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