Investigation of the interaction between bromocriptine and human serum albumin with spectroscopic techniques and computational approaches.

IF 2.7 3区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
Sevinc Ayla Ozsar, Cigdem Kanbes-Dindar, Fazal Rehman, Saharuddin B Mohamad, Bengi Uslu
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引用次数: 0

Abstract

Fluorescence and absorption spectroscopy coupled with molecular docking techniques were chosen to reveal the molecular relationship between bromocriptine (BRC), a dopamine agonist, and human serum albumin (HSA), the major carrier protein in the bloodstream. The gradual decrease of Stern-Volmer constant (KSV) with increasing temperatures noted that BRC induced quenching in HSA fluorescence occurred via a static quenching mechanism, thus indicating the formation of complexes between BRC and HSA. The changes observed in the UV-vis absorption spectra of HSA as a result of BRC addition and the fact that the biomolecular quenching rate constants (Kq) calculated for the BRC-HSA interaction are significantly larger than the highest value of the dynamic quenching rate constant also support this conclusion. Considering the experimentally obtained binding constant (Ka) values ​​(2.6 - 3.8 x 104 M-1), BRC appeared to bind to HSA with a moderate affinity. Analysis of thermodynamic data suggested the association of hydrophobic interactions, H-bonds and van der Waals forces as the main interaction forces in the BRC-HSA binding. It was determined by 3-D fluorescence spectra that the binding of BRC to the protein led to significant changes in the Tyr/Trp microenvironment of the protein. Docking analyses and drug displacement experiments identified that BRC likely binds to subdomain IIA (Site I) of HSA.

用光谱技术和计算方法研究溴隐亭与人血清白蛋白的相互作用。
采用荧光和吸收光谱结合分子对接技术,揭示了多巴胺激动剂溴隐亭(BRC)与血液中主要载体蛋白人血清白蛋白(HSA)之间的分子关系。Stern-Volmer常数(KSV)随温度升高而逐渐减小,说明BRC诱导HSA荧光猝灭是通过静态猝灭机制发生的,说明BRC与HSA之间形成了配合物。BRC对HSA紫外可见吸收光谱的影响以及BRC-HSA相互作用的生物分子猝灭速率常数(Kq)明显大于动态猝灭速率常数的最大值也支持了这一结论。考虑到实验得到的结合常数(Ka)值(2.6 - 3.8 x 104 M-1), BRC似乎以中等亲和力与HSA结合。热力学数据分析表明疏水相互作用、氢键和范德华力是BRC-HSA结合的主要相互作用力。通过三维荧光光谱测定,BRC与该蛋白结合导致该蛋白的Tyr/Trp微环境发生显著变化。对接分析和药物置换实验表明,BRC可能与HSA的IIA亚结构域(Site I)结合。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Journal of Biomolecular Structure & Dynamics
Journal of Biomolecular Structure & Dynamics 生物-生化与分子生物学
CiteScore
8.90
自引率
9.10%
发文量
597
审稿时长
2 months
期刊介绍: The Journal of Biomolecular Structure and Dynamics welcomes manuscripts on biological structure, dynamics, interactions and expression. The Journal is one of the leading publications in high end computational science, atomic structural biology, bioinformatics, virtual drug design, genomics and biological networks.
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