Investigating Interaction Between Biochanin A and Human Serum Albumin by Multi-spectroscopic and Molecular Simulation Methods

被引：0
作者：
Xue Z. [1 ]
Cheng A. [1 ]
Li Y. [1 ]
Yu W. [2 ]
Kou X. [1 ]
机构：
[1] School of Chemical Engineering and Technology, Tianjin University, Tianjin
[2] Medical Plant Lab, Tianjin Research Center of Agricultural Biotechnology, Tianjin
来源：
Transactions of Tianjin University | 2017年 / 23卷 / 4期
关键词：
Biochanin A; Human serum albumin; Interaction; Molecular dynamics simulation; Multi-spectroscopy;
D O I：
10.1007/s12209-017-0046-1
中图分类号：
学科分类号：
摘要：
Biochanin A (BCA), the most abundant isoflavone in chickpeas, presents a wide range of biological activities, such as hypolipidaemic, anti-oxidative, anti-proliferative, and estrogen-like effects. We investigated the interaction between BCA and human serum albumin (HSA) via several techniques. UV–Vis absorption spectroscopy verified the conformational variation of HSA after BCA addition, and fluorescence spectroscopy revealed the relevant binding parameters. Circular dichroism spectroscopy was used to estimate the secondary structural changes of HSA with and without BCA. Molecular docking and dynamics simulations were then applied to study the characteristics of HSA with BCA. Energy decomposition analysis was used to prove that Trp214 in subdomain IIA of HSA is the most likely binding site of BCA. Van der Waals forces and hydrophobic interactions may play important roles during the binding process. All of our results showed that BCA presents significant binding affinity to HSA, thus confirming that the role of HSA has as an efficient transporter of biomolecules. © 2017, Tianjin University and Springer-Verlag Berlin Heidelberg.
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页码：325 / 333
页数：8
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