Hydrophobic nanofibers: a peptide-based functional anti-fouling material

Abstract

Functional bioinspired materials have been developed by molecular self-assembly of a hydrophobic peptide. Two analogue peptides containing hydrophobic L-alanine, α-aminoisobutyric acid (Aib), L-phenylalanine and L-tyrosine deliver different supramolecular structures and functions. Peptide 1 containing L-phenylalanine adopts a β-turn conformation and self-assembles through intermolecular hydrogen bonds to form a supramolecular hydrophobic sheet-like structure. But peptide 2 with L-tyrosine adopts kink-like conformations and self-assembles to form a supramolecular hydrogen bonded helix-like architecture. Irrespective of the presence of the same peptide backbone conformation, only the side chain hydroxyl functional group has introduced a huge change in self-assembly pattern and function. The hydrophobic peptide 1 further self-assembled to form slippery nanofibers. The resulting surfaces show anti-sticking effects against water and exhibit anti-fouling properties, like inhibiting the growth of Escherichia coli.