A Peptide-Coated Gold Nanocluster Exhibits Unique Behavior in Protein Activity Inhibition
An DY(安德义); An, DY; Su, JG; Weber, JK; Gao, XY; Zhou, RH; Li, JY; Gao XY(高学云); Li JY(李敬源)
刊名JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
2015
卷号137期号:26页码:8412-8418
学科分类Chemistry
DOI10.1021/jacs.5b00888
通讯作者李敬源
文章类型Article
英文摘要Gold nanoclusters (AuNCs) can be primed for biomedical applications through functionalization with peptide coatings. Often anchored by thiol groups, such peptide coronae not only serve as passivators but can also endow AuNCs with additional bioactive properties. In this work, we use molecular dynamics simulations to study the structure of a tridecapeptide-coated Au-25 cluster and its subsequent interactions with the enzyme thioredoxin reductase 1, TrxR1. We find that, in isolation, both the distribution and conformation of the coating peptides fluctuate considerably. When the coated AuNC is placed around TrxR1, however, the motion of the highly charged peptide coating (+5e/peptide) is quickly biased by electrostatic attraction to the protein; the asymmetric coating acts to guide the nanocluster's diffusion toward the enzythe's negatively charged active site. After the AuNC comes into contact with TrxR1, its peptide corona spreads over the protein surface to facilitate stable binding with protein. Though individual salt bridge interactions between the tridecapeptides and TrxR1 are transient in nature, the cooperative binding of the peptide-coated AuNC is very stable, overall. Interestingly, the biased corona peptide motion, the spreading and the cooperation between peptide extensions observed in AuNC binding are reminiscent of bacterial stimulus-driven approaching and adhesion mechanisms mediated by cilia. The prevailing AuNC binding mode we characterize also satisfies a notable hydrophobic interaction seen in the association of thioredoxin to TrxR1, providing a possible explanation for the AuNC binding specificity observed in experiments. Our simulations thus suggest this peptide-coated AuNC serves as an adept thioredoxin mimic that extends an array of auxiliary structural components capable of enhancing interactions with the target protein in question.
类目[WOS]Chemistry, Multidisciplinary
收录类别SCI ; EI ; CA
WOS记录号WOS:000357964400025
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被引频次:25[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.ihep.ac.cn/handle/311005/228595
专题中国科学院高能物理研究所_多学科研究中心_期刊论文
中国科学院高能物理研究所_多学科研究中心
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An DY,An, DY,Su, JG,et al. A Peptide-Coated Gold Nanocluster Exhibits Unique Behavior in Protein Activity Inhibition[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,2015,137(26):8412-8418.
APA 安德义.,An, DY.,Su, JG.,Weber, JK.,Gao, XY.,...&李敬源.(2015).A Peptide-Coated Gold Nanocluster Exhibits Unique Behavior in Protein Activity Inhibition.JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,137(26),8412-8418.
MLA 安德义,et al."A Peptide-Coated Gold Nanocluster Exhibits Unique Behavior in Protein Activity Inhibition".JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 137.26(2015):8412-8418.
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