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首页> 外文期刊>Luminescence: The journal of biological and chemical luminescence >Synthesis and study on the binding of thiazol-2(3H)-ylidine derivative with human serum albumin using spectroscopic and molecular docking methods
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Synthesis and study on the binding of thiazol-2(3H)-ylidine derivative with human serum albumin using spectroscopic and molecular docking methods

机译：用谱和分子对接方法合成研究与人血清白蛋白与人血清白蛋白衍生物的结合

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摘要

In this article, a facile and convenient synthesis of thiazol-2(3H)-ylidine derivatives of fatty acid (3a-c) is described. The binding of N-(4,5-dimethyl-3-penylthiazol-2(3H)-ylidine)octadec-9-enehydrazide (3a) with human serum albumin (HSA) is explored using various spectral methods and molecular docking. Fluorescence quenching results show that 3a induces conformational changes in HSA and the polarity around the tryptophan residues is increased. Stern-Volmer quenching plots at different temperatures (298, 305 and 312K) show that the fluorescence quenching mechanism is static quenching. Synchronous fluorescence, 3D fluorescence spectra, circular dichroism and Fourier transform infrared spectroscopy are used to determine the structural change in HSA on interaction with 3a. Forster resonance energy transfer analysis shows that the binding distance (r(0)=2.78nm) between HSA (Trp214) and 3a is within the of range 2-8nm for quenching to occur. The molecular docking study also confirms that 3a is located in subdomain IIA (site I) of HSA and is stabilized by hydrogen bonding and hydrophobic forces.
机译：在本文中，描述了脂肪酸（3A-C）的噻唑-2（3H）衍生物的容易和方便的合成。利用各种光谱方法和分子对接探索N-（4,5-二甲基-3-丙二醇-2（3H） - 烯酮-2（3H） - 烯酮-2（3A）与人血清白蛋白（HSA）的结合。荧光猝灭结果表明，3A诱导HSA的构象变化，并且围绕色氨酸残留物的极性增加。在不同温度（298,305和312K）的船尾淬火图表明荧光猝灭机构是静态淬火。同步荧光，3D荧光光谱，圆形二色性和傅立叶变换红外光谱用于确定HSA与3A相互作用的结构变化。 Forster Exonance能量转移分析表明，HSA（TRP214）和3A之间的结合距离（R（0）= 2.78nm）在2-8nm的范围内以进行淬火。分子对接研究还证实3A位于HSA的亚域IIa（位点I）中，并通过氢键和疏水力稳定。

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