Collagen Mimicry with A Short Collagen Model Peptide.

Mimicking triple helix and fibrillar network of collagen through collagen model peptide(CMP) with short GPO tripeptide repeats is a great challenge. Herein, we present a minimalistic CMP comprising only five GPO repeats[(GPO) 5 ]. Our novel approach involves the fusion of ultrashort peptide with the synergetic power of π-system and β-Sheet formation to short CMP(GPO) 5 . Accordingly, a hydrogel-forming, Fmoc-functionalized ultrashort peptide (NFGAIL) was fused at the N-terminus and phenylalanine at the C-terminus of (GPO) 5 (Fmoc-NFGAIL-(GPO) 5 -F-COOH,FmP-5GPO). At room temperature, it forms a robust triple helix in aqueous buffer solution and has a relatively high melting point of 35°C. The fluorenyl motif stabilizes the triple helix by aromatic π-π interactions as in its absence, triple helix was not formed. NFGAIL, which forms a β-sheet, also aids in triple helix stabilization via intermolecular hydrogen bonding and hydrophobic interactions. FmP-5GPO forms highly entangled fibrils with a micrometer length and a diameter of 13.2±2.8 nm, which have excellent cell viability. The achievement of stable triple helix and fibrils in such a short CMP(FmP-5GPO) sequence is a challenging feat, and its significance in CMP-based biomaterials is undeniable. The present strategy highlights the potential for developing new CMP sequences through intelligent tuning of fusion peptides and GPO repeats. This article is protected by copyright. All rights reserved.