Effect of the phosphorylation structure in casein phosphopeptides on the proliferation, differentiation, and mineralization of osteoblasts and its mechanism
Wanying Zhong, Jian He, Wen Huang, Guangling Yin, Guo Liu, Yong Cao, Jianyin Miao
Abstract
molecular docking showed that the binding force of the P5-EGFR complex was stronger than that of the P5-0-EGFR complex, which was significantly related to the phosphorylation structure in P5 and might be an important reason for osteoblast proliferation. In conclusion, the phosphorylation structure and amino acid composition in P5 stimulated the osteogenic activity of MC3T3-E1 cells, and could be expected to be a functional food for the prevention of osteoporosis.
Topics & Concepts
RUNX2PhosphorylationChemistryAlkaline phosphataseOsteoblastMineralization (soil science)Cellular differentiationCell growthCalciumCaseinBiochemistryCell biologyEnzymeBiologyIn vitroOrganic chemistryNitrogenGeneProtein Hydrolysis and Bioactive PeptidesPhytase and its ApplicationsBone and Dental Protein Studies