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首页> 外文期刊>Human and Experimental Toxicology >Characterization of the interaction between human serum albumin and diazinon via spectroscopic and molecular docking methods
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Characterization of the interaction between human serum albumin and diazinon via spectroscopic and molecular docking methods

机译：通过光谱和分子对接方法表征人血清白蛋白和二嗪蛋白的相互作用

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摘要

Human serum albumin (HSA) is a soluble blood protein which binds to small molecules (such as drugs and toxins) and transfers them within the blood circulation. In this research, the interaction of diazinon, as a toxic organophosphate, with HSA was investigated. Various biophysical methods such as fluorescence, ultraviolet-visible (UV-vis), Fourier transform infrared spectroscopy, and molecular docking were utilized to characterize the binding properties of diazinon to HSA under physiological-like condition. The UV-vis spectroscopy showed that the absorption increased and the fluorescence intensity of HSA decreased regularly with regard to the gradual increases of the concentrations of diazinon. Due to the binding constant of (k(a) = 3.367 x 10(+4) M-1), the -helix structure for the first day and 35 days of incubation were obtained 66.09-55.4% and 59.99-46.48%, respectively, and their amounts in other secondary structures (-sheet, -anti, and random (r) coils) were increased. The molecular docking revealed a good binding site in HSA (Trp-214) for diazinon which was related to the considerable alterations in HSA secondary and tertiary structures. There is a close relationship between the secondary structure of protein and its biological activity and after 35 days of incubation, the high toxic concentrations of diazinon can make HSA to be partially unfolded and lose its structure.
机译：人血清白蛋白（HSA）是一种可溶性血液蛋白，其与小分子（如药物和毒素）结合，并将它们转移到血液循环内。在该研究中，研究了一种具有HSA的Diazinon作为有毒有机磷酸酯的相互作用。使用诸如荧光，紫外 - 可见（UV-VIS），傅里叶变换红外光谱和分子对接的各种生物物理方法，以在生理样条件下表征Diazinon至HSA的结合特性。 UV-Vis光谱表明，在逐渐增加的二嗪酮的慢性增加方面，HSA的吸收增加和荧光强度降低。由于（k（a）= 3.367×10（+ 4）m-1）的结合常数，分别为第一天和35天孵育的-helix结构分别为66.09-55.4％和59.99-46.48％并且它们在其他二级结构（ - 分号， - antid和随机（R）线圈中的量增加。分子对接揭示了HSA（TRP-214）中的良好结合位点，用于双子蛋白，其与HSA二级和三级结构中相当大的改变有关。蛋白质及其生物活性的二级结构与孵育35天后的关系密切的关系，毒性浓度的高毒性浓度可以使HSA部分展开并失去其结构。

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