National Engineering Research Center of Seafood, School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, PR China.
National Engineering Research Center of Seafood, School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, PR China.
Food Chem. 2020 Apr 25;310:125867. doi: 10.1016/j.foodchem.2019.125867. Epub 2019 Nov 8.
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.
磷酸化可以改善蛋白质/肽的功能特性，并且由于其富含磷酸化位点，因此可能用于提高鲱鱼卵肽的功能。本研究旨在研究磷酸化对鲱鱼卵肽钙结合能力的影响，并研究鲱鱼卵磷酸肽（HEPPs）-钙复合物的构象结构和分子间力。与非磷酸化变体相比，发现 HEPPs 具有更高的钙结合活性。这一发现可能归因于钙离子与 HEPPs 中引入的磷酸基团之间的相互作用。钙离子有利于 HEPPs 上β-折叠结构的形成，并诱导结构折叠，从而组装成球形纳米颗粒。HEPPs-Ca 纳米颗粒的构象主要通过疏水相互作用、氢键和静电相互作用形成和稳定。
