Interaction of mercury ion (Hg2+) with blood and cytotoxicity attenuation by serum albumin binding
Interaction of mercury ion (Hg2+) with blood and cytotoxicity attenuation by serum albumin binding
复制标题
汞离子 (Hg2 ) 与血液的相互作用以及通过血清白蛋白结合减弱细胞毒性
DOI：
10.1016/j.jhazmat.2021.125158
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发表时间：
2021
影响因子：
13.6
通讯作者：
Zongwei Cai
中科院分区：
文献类型：
--
作者：
Shanjun Song;Yiling Li;Qian Liu;Huiyu Wang;Penghui Li;Jianbo Shi;Ligang Hu;Haiyan Zhang;Yuanchen Liu;Kun Li;Xingchen Zhao;Zongwei Cai
血液中的汞反映了从组织中获得的汞量，这是暴露水平的一个指标。在这里，我们证实，Hg 2+引起溶血作用在高浓度下，而在轻浓度下，大多数离子结合到人血清白蛋白（HSA）。Hg 2+与HSA的结合机制研究表明，Hg 2+的存在对HSA的结构产生了明显的扰动，并以动态和静态混合的方式猝灭蛋白质的荧光。Hg 2+优先与半胱氨酸和胱氨酸结合，其中R S S R结构负责通过稳定α-螺旋束来维持蛋白质的结构。金属-蛋白质相互作用减轻了A498细胞系所隐藏的细胞毒性。这些基础性和全面的数据有助于阐明和理解重金属与蛋白质的识别和结合机制，以及对人类和环境的潜在风险。
Blood mercury reflects the amount available from tissues, which is an indication of the exposure level. Here we confirm that Hg2+caused hemolytic effects at high concentrations; while at light concentrations, most of the ions were bound to human serum albumin (HSA). The binding mechanism of Hg2+to HSA has been investigated, which indicated that the presence of Hg2+significantly perturbed the structure of HSA and quenched the fluorescence of protein in a hybrid dynamic and static mode. Hg2+was preferably bound to cysteine and cystine, where the R‒S‒S‒R structure is responsible for maintaining the protein’s structure by stabilizing the α-helical bundles. The metal-protein interaction mitigated the cellular toxicity as concealed by A498 cell lines. The fundamental and comprehensive data in this work is beneficial to elucidating and understanding the identification and binding mechanisms of heavy metals with proteins, as well as possible risks on human beings and the environment.