Zn2+-Coordination-Driven Helical Dodecapeptide Assembly Hydrogel

Abstract

Peptide-based hydrogels have great potential in food industry and biomedical field because of their good biocompatibility and three‐dimensional printability. Molecular mechanisms and mechanical properties of peptide hydrogels are crucial for determining whether these hydrogels are potentially suitable for the food field. Polypeptide hydrogels are usually composed of fibrin hydrogel and RADA16-based peptides, while hydrogels formed by self‐assembly of food derived‐peptides are rarely reported. Peptide hydrogels were usually assembled from β-sheet structure, designing hydrogels directly from helical structures in water is a challenge in self-assembly. In this study, researchers have successfully designed a functional dodecapeptide, which can assemble into supra-molecular hydrogels with helical structure. This assembly is directed by Zn2+ chelation without any chemical modifications. Face-to-face packed dimer of assembling subunits were consisted by Glu5, Glu7, Glu9, and Glu11. Additionally, guanidine moiety in Arg12 formed aromatic interactions resulting in the disruption of the 310-helix and the formation of a turn structure in P-Zn-9. The findings provide an efficient strategy to achieve both helical structure peptides and Zn2+ chelating capacity in order to prepare assembled hydrogels.

Keywords: peptides, Zinc, Assembly, Hydrogels, Chelating sites, Nuclear magnetic resonance spectroscopy