Synthesis of enzymatically crosslinkable peptide-poly(L-lysine) conjugate and creation of bio-inspired hybrid fibers.

Abstract

Poly(L-lysine)s having an Nepsilon-substituted tetrapeptide, Lys-Gly-Tyr-Gly, were synthesized by the coupling of the protected tetrapeptide active ester, Boc-Lys(Z)-Gly-Tyr(Bzl)-Gly (4-hydroxyphenyl)dimethylsulfonium methylsulfate and Nepsilon-group of the poly(L-lysine) side chain. The Nepsilon-substituted tetrapeptide functions as the substrate of tyrosinase and is responsible for the enzyme-mediated interpolymer cross-linking. The degree of Nepsilon-substitution (DS) was mostly controlled by changing the stoichiometry between the Nepsilon-amino groups of the parent poly(L-lysine) and the protected tetrapeptide active ester. Two kinds of samples having DS values of 8.6 and 18 mol-% were prepared. The resulting cationic Nepsilon-(Lys-Gly-Tyr-Gly)-poly(L-lysine) (abbreviated as PLL(GYGK)) was spun into hybrid fibers with the anionic polysaccharide gellan via a polyionic complexation reaction at the interface between aqueous solutions of the two polymers. The mechanical strengths of the PLL(GYGK)-gellan hybrid fibers were superior to those of the original poly(L-lysine)-gellan fibers. The mechanical strength of the hybrid fibers further increased upon the tyrosinase-mediated cross-linking reaction of the PLL(GYGK). This result indicates that the covalent cross-bridge formation between the Nepsilon-substituted peptides significantly contributed to reinforcement of the hybrid fibers. The present study affords a new methodology for reinforcement inspired by a biological process.