Chinese Journal of Applied Chemistry ›› 2021, Vol. 38 ›› Issue (8): 1014-1021.DOI: 10.19894/j.issn.1000-0518.200377

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Interaction Between Preservative Benzoic Acid and Human Serum Albumin

DENG Pei-Yuan1, YUAN Wei2, LI Chang-Kan1, CHEN Long-Xin1, YANG Ying-Ying1*   

  1. 1Biological Species Resource Research Key Laboratory, Zhengzhou Normal University, Zhengzhou 450044, China
    2Institute of Environmental and Municipal Engineering, North China University of Water Resources and Electric Power, Zhengzhou 450046, China
  • Received:2020-12-15 Revised:2021-04-10 Published:2021-08-01 Online:2021-10-01
  • Supported by:
    National Natural Science Foundation of China (No.NSFC32071447), the Key R&D and Promotion Projects of Henan Province (No.212102110462)

Abstract: In order to study the transport and degradation mechanism of food preservative benzoic acid in the body, the interaction between benzoic acid and human serum albumin (HSA) is investigated by fluorescence spectroscopy, molecular docking, molecular dynamics simulation and alanine mutation scanning under the body physiological conditions. Results show that the quenching of HSA by benzoic acid is a static process, the binding constant KA is larger than 104 L/mol at different temperatures, the number of binding sites is approximate to 1, and the binding takes place primarily in site II; Van't Hoff equation and molecular dynamics indicate that the electrostatic force is the main promoting force, the polar solvation energy is the main resistance force, and the binding is a spontaneous reaction with free energy reduction; the molecular docking results show that benzoic acid form a hydrogen bond with ARG186. Besides, ASP108, GLN425 and GLV459 are proved to be the key amino acids for binding through alanine mutation scanning calculation.

Key words: Benzoic acid, Human serum albumin, Fluorescence quenching, Molecular docking, Molecular dynamics simulation

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