Studies of the β-sheet mediated self-assembly of designed synthetic peptides of general formula PhCO-Gly-Xx-OCH2Ph and the possible role of aromatic π-π interactions in the self-assembly

Abstract

A set of three peptides 1-3 of general formula PhCO-Gly-Xx-OCH 2Ph, where Xx is Gly in peptide 1, Ala in 2 and Aib (α-animo isobutyric acid) in 3 has been chosen to study the selfassembly and the morphology of the solid biomaterials. FT-IR and single crystal X-ray diffraction studies reveal that the peptides 1-3 self-assemble to form supramolecular p-sheet structures through intermolecular hydrogen bonds and aromatic π-π interactions. Field emission scanning electron micrographs (FE-SEM) of the dried materials of the peptides 1-3 show the formation of flat ribbon like structures which are formed through β-sheet mediated selfassembly.