Title
Calcium binding to herring egg phosphopeptides: Binding characteristics, conformational structure and intermolecular forces
Author
Na Sun, Yixing Wang, Zhijie Bao, Pengbo Cui, Shan Wang, Songyi Lin
Year
2020
Journal
Food Chemistry
Abstract
Phosphorylation could improve functional characteristics of proteins/peptides, and might be used in the functional improvement of herring egg peptides owing to their enriched phosphorylation sites. The present study aimed to study the effect of phosphorylation on calcium-binding ability of herring egg peptides, and investigate the conformational structure and intermolecular forces of herring egg phosphopeptides (HEPPs)-calcium complex. The HEPPs were found to be superior in calcium-binding activities, as compared to the non-phosphorylated variant. This finding might be attributed to the interaction between calcium ions and the introduced phosphate groups of HEPPs. Calcium favored the formation of β-sheet structure on the HEPPs and induced structural folding, thus assembling into spherical nanoparticles. The conformation of HEPPs-Ca nanoparticles was formed and stabilized mainly by hydrophobic interaction, hydrogen bonds and electrostatic interaction.
Instrument
J-1500
Keywords
Circular dichroism, Secondary structure, Ligand binding, Food science, Biochemistry