Interaction of glutathione with bovine serum albumin: Spectroscopy and molecular docking
Interaction of glutathione with bovine serum albumin: Spectroscopy and molecular docking
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DOI：
10.1016/j.foodchem.2016.02.026
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发表时间：
2016-07-01
期刊：
影响因子：
8.8
通讯作者：
Panahi-Azar, Vahid
中科院分区：
文献类型：
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作者：
Jahanban-Esfahlan, Ali;Panahi-Azar, Vahid
本研究旨在利用紫外-可见（UV-vis）吸收、模拟生理条件（pH 7.4）下的荧光光谱和分子对接方法研究谷胱甘肽与牛血清白蛋白（BSA）的相互作用。荧光光谱结果表明，加入谷胱甘肽后，牛血清白蛋白的荧光强度通过静态猝灭机制明显降低。荧光猝灭与bsa -谷胱甘肽络合物的形成有关。谷胱甘肽与牛血清白蛋白相互作用的K-SV、K-a和K-b值约为10(5)。热力学参数包括焓变(H)、熵变(S)和吉布自由能(G)，由范霍夫方程确定。这些值表明，氢键和范德华力是谷胱甘肽与牛血清蛋白结合和络合物稳定的主要相互作用。谷胱甘肽与牛血清白蛋白的相互作用是自发的。采用紫外-可见光谱法测定谷胱甘肽对牛血清白蛋白构象的影响。此外，利用ArgusLab作为分子对接程序，将谷胱甘肽对接到BSA中。认识到谷胱甘肽结合在BSA II结构域的IIA亚结构域口袋内。(C) 2016 Elsevier Ltd.版权所有。
This study aims to investigate the interaction between glutathione and bovine serum albumin (BSA) using ultraviolet-visible (UV-vis) absorption, fluorescence spectroscopies under simulated physiological conditions (pH 7.4) and molecular docking methods. The results of fluorescence spectroscopy indicated that the fluorescence intensity of BSA was decreased considerably upon the addition of glutathione through a static quenching mechanism. The fluorescence quenching obtained was related to the formation of BSA-glutathione complex. The values of K-SV, K-a and K-b for the glutathione and BSA interaction were in the order of 10(5). The thermodynamic parameters including enthalpy change (Delta H), entropy change (Delta S) and also Gibb's free energy (Delta G) were determined using Van't Hoff equation. These values showed that hydrogen bonding and van der Waals forces were the main interactions in the binding of glutathione to BSA and the stabilization of the complex. Also, the interaction of glutathione and BSA was spontaneous. The effects of glutathione on the BSA conformation were determined using UV-vis spectroscopy. Moreover, glutathione was docked in BSA using ArgusLab as a molecular docking program. It was recognized that glutathione binds within the sub-domain IIA pocket in domain II of BSA. (C) 2016 Elsevier Ltd. All rights reserved.