Molecular Design of β-Hairpin Peptides for Material Construction

Abstract

AbstractSelf-assembled materials composed of β-sheet forming peptides hold promise as therapeutics and novel biomaterials. This article focuses on the design and engineering of amphiphilic peptide sequences, especially β-hairpins. Peptides can be designed to intramolecularly fold and then self-assemble on cue, affording hydrogels rich in β-sheet structure. Hydrogels having distinct material properties can be designed at the molecular level by modulating either the peptide's sequence or the environmental stimulus used to trigger folding and assembly, leading to gelation.