Studying the Effects of Cysteine Residues on Protein Interactions with Silver Nanoparticles.
Studying the Effects of Cysteine Residues on Protein Interactions with Silver Nanoparticles.
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DOI：
10.1021/jp512440z
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发表时间：
2015
期刊：
影响因子：
--
通讯作者：
Zhang D
中科院分区：
文献类型：
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作者：
Siriwardana K;Wang A;Gadogbe M;Collier WE;Fitzkee NC;Zhang D
研究蛋白质和有机硫醇与银纳米粒子（AgNP）的相互作用对于理解AgNP的纳米毒性、抗菌活性和材料制造是重要的。本文报道的是还原和氧化的蛋白质半胱氨酸残基对蛋白质与银纳米颗粒相互作用的影响的系统研究。模型蛋白包括分别含有0、1或2个还原半胱氨酸残基的野生型和突变蛋白GB 3变体。还包括含有总共34个氧化（二硫键连接）半胱氨酸残基和1个还原半胱氨酸残基的牛血清白蛋白（BSA）。蛋白质半胱氨酸含量对蛋白质/AgNP结合的动力学没有可检测的影响。然而，只有含有还原的半胱氨酸残基的蛋白质诱导显著的AgNP溶解。蛋白质可以减慢，但不能阻止随后加入的有机硫醇诱导的AgNP溶解。在这项工作中提供的见解是重要的AgNP在生物流体中，富含蛋白质和氨基酸硫醇的稳定性的机械理解。
Studies of protein and organothiol interactions with silver nanoparticles (AgNPs) are important for understanding AgNP nanotoxicity, antimicrobial activity, and material fabrications. Reported herein is a systematic investigation of the effects of both reduced and oxidized protein cysteine residues on protein interactions with AgNPs. The model proteins included wild-type and mutated protein GB3 variants that contain 0, 1, or 2 reduced cysteine residues, respectively. Bovine serum albumin (BSA) that contains a total of 34 oxidized (disulfide-linked) cysteine residues and one reduced cysteine residue was also included. Protein cysteine content has no detectable effect on the kinetics of protein/AgNP binding. However, only proteins that contain reduced cysteine residues induce significant AgNP dissolution. Proteins can slow down, but do not prevent the AgNP dissolution induced by subsequently added organothiols. The insights provided in this work are important to the mechanistic understanding of AgNP stability in biofluids that are rich in proteins and amino acid thiols.