Citation: Guo Chune, Guo Xiaomi, Chu Wubo, Jiang Nan, Li He. Spectroscopic study of conformation changes of bovine serum albumin in aqueous environment[J]. Chinese Chemical Letters, ;2019, 30(6): 1302-1306. doi: 10.1016/j.cclet.2019.02.023 shu

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

Guo Chune ^a,b ,
Guo Xiaomi ^a,b ,
Chu Wubo ^a ,
Jiang Nan ^a,b ,
Li He ^a,b,*,

a.
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
b.
College of Materials Science and Optoelectronic Technology, University of Chinese Academy of Sciences, Beijing 100049, China

lihe@nimte.ac.cn

Received Date: 24 January 2019
Revised Date: 19 February 2019
Accepted Date: 22 February 2019
Available Online: 23 June 2019

Figures(5)

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.
- BSA,
- Secondary structure change,
- Calcium cation,
- ATR-FTIR,
- Raman
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