Spectroscopic investigations of the interaction of the anti‑hypertension drug valsartan with human serum albumin

Jing,Jian; Qu,Xin; Tu,Zhi; Zheng,Chenhoo; Zheng,Zhicheng

doi:10.3892/mmr.2014.2129

Spectroscopic investigations of the interaction of the anti‑hypertension drug valsartan with human serum albumin

Authors:
- Jian Jing
- Xin Qu
- Zhi Tu
- Chenhoo Zheng
- Zhicheng Zheng
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Affiliations: Department of Bioorganic and Biological Chemistry, Beijing Key Lab, Beijing Normal University, Beijing 100875, P.R. China
Published online on: April 9, 2014 https://doi.org/10.3892/mmr.2014.2129
Pages: 2191-2196

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Abstract

The aim of the present study was to investigate the interaction between valsartan, an anti‑hypertension drug, and human serum albumin (HSA) using spectroscopic techniques, including fluorescence, ultraviolet‑visible absorption, synchronous fluorescence and circular dichroism (CD). The results demonstrated that valsartan and HSA form a complex and that a static quenching mechanism occurs. In addition, the binding constant and the number of binding sites for valsartan on HSA were analyzed. Hydrophobic interactions and hydrogen bonds were the predominant forces in the association reaction based on thermodynamic parameters. The distance between the donor (HSA) and the acceptor (valsartan) was 1.994 nm as derived from Forster's theory. Alterations in the secondary structure of HSA in the presence of valsartan were assessed using synchronous fluorescence and CD. This study provides an enhanced understanding of the pharmacodynamic effects of valsartan on the physiologically important protein HSA.

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