Interaction Between Progesterone and Bovine Serum Albumin by Fluorescence Spectrum and Molecular Docking

被引：0
|
作者：
Yang S.-L. [1 ]
Liao X.-P. [1 ]
Fan X. [2 ]
Tuo X. [1 ]
机构：
[1] College of Chemistry, Nanchang University, Nanchang
[2] School of Pharmacy, Nanchang University, Nanchang
来源：
Faguang Xuebao/Chinese Journal of Luminescence | 2019年 / 40卷 / 11期
基金：
中国国家自然科学基金;
关键词：
Bovine serum albumin; Fluorescence spectrum; Interaction; Molecular docking; Progesterone;
D O I：
10.3788/fgxb20194011.1439
中图分类号：
学科分类号：
摘要：
Progesterone(PROG) is a common drug for treatment of threatened abortion in clinical practice, but its transport mechanism in human body is still unclear. Here, fluorescence spectrum, infrared spectrum, and molecular docking were employed to comprehensively analyze the mechanism underlying the interaction between PROG and bovine serum albumin (BSA). The results indicated that a stable PROG-BSA complex was formed and van der Waals forces played a major role in this binding process. The order of magnitude of the binding constants (Ka) was 1.423×104 L•mol-1 at normal body temperature of human. Solution experiments showed that the binding site for PROG was located at Sudlow site I of BSA, and the distance between PROG and BSA was obtained(r=1.63 nm) according to the Förster theory of non-radiative energy transfer. Infrared spectrum results revealed the changes in secondary structure of the protein upon interaction with PROG. The results of Ligplus+ highlighted the role of hydrogen bonds in the bind process whereas in well agreement with solution experiments. The data of spectrum and molecular docking experiments confirmed each other, which provided data support for revealing the transport and storage process of PROG in human body. This work will be helping us to understand the binding mode of PROG-BSA system and provide a new insight about the effect of PROG on human health. © 2019, Science Press. All right reserved.
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页码：1439 / 1445
页数：6
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