白杨素与不同构型人血清白蛋白的作用机制

doi:10.3866/PKU.WHXB201310311

Abstract

Abstract:

The mechanism of the interaction between Chrysin (CHR) and human serum albumin (HSA) was investigated using various spectroscopic techniques. It was found that CHR can induce HSA fluorescence emission quenching by static process. Additionally, HSA caused a significant red shift in the ultraviolet absorption of CHR. This indicated that binding with a protein can result in dissociation of the phenolic hydroxyl in CHR. HSA can also cause CHR fluorescence emission. The binding constants of CHR and HAS were calculated based on the fluorescence quenching and emission modes. The results obtained using these two methods were consistent. The binding constant (K_A) values at pH 7.4 were (9.97±0.24)×10⁴ and (9.75±0.11)×10⁴ L·mol^-1, respectively; and the ratio of combination was 1:1. The binding constants decreased gradually with decreasing the pH value. This is related to conformational changes in the protein. The protein is partly denatured at pH 3.5, with the site Ⅱ in the HSA opening chain. It was found that CHR was located at site I, which is in subdomain ⅡA of HAS. Based on molecular modeling, the mechanism of the interaction between CHR and HAS was investigated.

Key words: Chrysin, Human serum albumin, Fluorescence, pH effect, Molecular modeling

LIU Yuan, LONG Mei, XIE Meng-Xia. Mechanism of Interaction between Chrysin and Different Configurations of Human Serum Albumin[J]. Acta Phys. -Chim. Sin. 2013, 29(12), 2647-2654. doi: 10.3866/PKU.WHXB201310311

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Mechanism of Interaction between Chrysin and Different Configurations of Human Serum Albumin

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