Spectroscopic study of conformation changes of bovine serum albumin in aqueous environment

作     者：Chune Guo Xiaomi Guo Wubo Chu Nan Jiang He Li 

作者机构：Key Laboratory of Marine Materials and Related Technologies CAS Zhejiang Key Laboratory of Marine Materials and Protective Technologies Ningbo Institute of Materials Technology and Engineering Chinese Academy of Sciences Ningbo 315201 China College of Materials Science and Optoelectronic Technology University of Chinese Academy of Sciences Beijing 100049 China 

出 版 物：《Chinese Chemical Letters》 (中国化学快报（英文版）)

年 卷 期：2019年第30卷第6期

页      面：1302-1306页

核心收录：

学科分类：07[理学] 0703[理学-化学] 

基　　金：financial support by the financial support by the National Natural Science Foundation of China(No. 21675165) 

主　　题：BSA Secondary structure change Calcium cation ATR-FTIR Raman 

摘      要：The secondary structural changes of bovine serum albumin (BSA) aqueous solutions with and without calcium cations were investigated by attenuated total reflection-Fourier transform infrared (ATR-FTIR) technology. The spectra of BSA solution and BSA dry powder were mainly reflected the formation of hydrogen bonds between water and BSA. Further investigation indicated that the concentrations of calcium cations in BSA aqueous solution also affected the secondary structural change of the protein. Amide I band was red shifted and amide II band was blue shifted in aqueous environment compared with the dry BSA powder, and the addition of calcium cations further changed the amide bands position, which led to the change of the secondary structure. The result was coinciding with the Raman spectroscopy.