合浦珠母贝无定形碳酸钙结合蛋白功能性肽段筛选及体外功能探究

通过预测、筛选并合成合浦珠母贝无定形碳酸钙结合蛋白(ACCBP)潜在的功能性肽段,发现位于其 C末端含乙酰胆碱结合位点保守区域的多肽具有显著的生物矿化功能;体外碳酸钙结晶速度实验显示该多肽能够延缓碳酸钙的结晶;体外碳酸钙结晶实验显示其能够显著影响方解石晶体的晶貌,使得方解石晶体的边缘呈现出阶梯状台阶现象;体外模拟间液离子环境碳酸钙结晶实验显示其能够抑制文石晶体成核或促进已成核文石晶体生长,使得实验组中的文石晶体颗粒数量显著减少并多呈现球形.结果提示了 ACCBP 上乙酰胆碱结合位点不仅能够直接参与生物矿化,并且很可能是其参与矿化的重要区域

Screening and Identifacation of Mineral Modulation Sequences Derived from ACCBP,an Extrapallial Fluid Protein of Pinctada fucata

Amorphous Calcium Carbonate Binding Protein(ACCBP) is responsible for maintaining the orderly morphology of nacre lamellae and stabilizing the CaCO3 supersaturated extrapallial fluid of the pearl oyster,Pinctada fucata.Since purification and characterization of ACCBP is very difficult and other proteins are involved in biomineralization,ACCBP plays an important role in the process of remaining unclear.The development of Bioinformatics and peptide synthetic technology proved a remedy to solve this problem by studying the effects of peptides originated from ACCBP.Through the prediction of the secondary structure and other structure character of ACCBP,three peptides were selected with peculiar structure respectively.The present in vitro experiments indicate that the acetylcholine binding sites is vital to ACCBP.This is also the first report that acetylcholine binding sites can directly participate in the biominerlization.