Human Fetuin-A Treatment for Demineralization of Arteriosclerosis

摘要

The lack of Ca detected by XPS for the Fetuin-A/ACC samples indicates Fetuin-A has bound with the CaCO_3 nanoparticles forming a protein coat during calciprotein particle (CPP) development and subsequent mineral stabilization. ATR-FTIR analysis of the Fetuin-A/ACC complex showed a loss of the Amide Ⅱ peak, indicating protein absorption through the amide group onto the nanoparticles. The observed UV/Vis shifts suggest that specific amino acid residues, tyrosine and tryptophan, participate in the ability of Fetuin-A to stabilize ACC growth and aggregation. These results support the hypothesis that Fetuin-A forms a protein coat around calcium mineral in order to stabilize and inhibit further growth.