Coiled-coil scallops (Chlamys farreri) peptide hydrogel with metal ionic and temperature tunable assembly

Abstract

Self-assembly of peptides is a powerful method of preparing nanostructured materials. Peptides frequently utilize charged groups as a convenient switch for controlling assembly state by pH, ionic strength or temperature. In this study, the molecular properties and gel-forming ability of Chlamys farreri protein hydrolysates were studied. According to self-assembled theory, the presence of isoleucine at position ‘a’ and leucine at ‘d’ causes a switch between coiled-coil structures. Compared to P-2-CG, the components of α-helix (23.60 ± 0.56%) were changed into β-sheet (4.83 ± 2.86%) in the secondary structure of the hydrogel induced by ZnCl2. NMR siginals appeared at high field,which indicated hydrogen bonds were formed between P-2-CG and solvent environments at 20 °C. With temperature going up, the hydrogen bonds were broken and nanofibrils were changed into dense aggregates. We expected that P-2-CG could provide a new candidate for preparing metal-induced nanofibers or hydrogels with further applications in food industry.