Citation: GUO Xiao-Mi, ZHANG Xiao-Xuan, CHU Wu-Bo, JIANG Nan, LI He. Infrared Spectroscopic Study of Pepsin Secondary Structure Changes on Surfaces[J]. Chinese Journal of Analytical Chemistry, ;2020, 48(9): 1273-1278. doi: 10.19756/j.issn.0253-3820.201189 shu

Infrared Spectroscopic Study of Pepsin Secondary Structure Changes on Surfaces

GUO Xiao-Mi ^1,2, ,
ZHANG Xiao-Xuan ^1,2 ,
CHU Wu-Bo ¹ ,
JIANG Nan ¹ ,
LI He ^1,2

1.
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;
2.
College of Materials Science and Optoelectronic Technology, University of Chinese Academy of Sciences, Beijing 100049, China

Received Date: 8 April 2020
Revised Date: 18 June 2020

Fund Project: This work was supported by the National Natural Science Foundation of China (No. 21675165).

Pepsin is an extremely important digestive enzyme in the stomach of mammals, which breaks down proteins in food by cutting off specific peptide bonds into amino acids. Pepsin is very sensitive to the pH of surroundings as a kind of acid protease, so the purpose of this experiment is to investigate the influence on the secondary structure of pepsin under various pH values and surfaces by Fourier transform infrared spectroscopy (FTIR) technology. The result shows that with the increase of pH, the percentage of β-sheet increases and reaches maximum in pH 3 to 7 and decreases when the solution is basic. The percentage of random coil is opposite to the β-sheet. When the ATR crystal surface is coated with TiO₂, the percentage of β-sheet is much greater than other secondary structures. Moreover, with the change of pH, the percentage of each secondary structure has no significant change. At the same time, quantitative analysis shows that the interaction between pepsin and TiO₂ is beneficial to the adsorption of pepsin on surface. It indicates that the functional groups can also affect the conformation of pepsin on the surface.
- Pepsin,
- Secondary structure,
- pH value,
- Infrared spectra,
- Titanium dioxide
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