A Peptide-Coated Gold Nanocluster Exhibits Unique Behavior in Protein Activity Inhibition
文献类型：期刊论文
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| 作者 | 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)
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| 刊名 | JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
 ; JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
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| 出版日期 | 2015 ; 2015 |
| 卷号 | 137期号:26页码:8412-8418 |
| ISSN号 | 0002-7863 |
| DOI | 10.1021/jacs.5b00888 |
| 通讯作者 | 李敬源 ; 李敬源 |
| 文献子类 | 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.; 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. |
| 学科主题 | Chemistry ; Chemistry |
| 类目[WOS] | Chemistry, Multidisciplinary |
| 收录类别 | SCI ; EI ; CA |
| WOS研究方向 | Chemistry, Multidisciplinary |
| 语种 | 英语 |
| WOS记录号 | WOS:000357964400025 ; WOS:000357964400025 |
| 公开日期 | 2016-05-03 |
| 源URL | [http://ir.ihep.ac.cn/handle/311005/228595]  |
| 专题 | 中国科学院高能物理研究所 |
| 推荐引用方式 GB/T 7714 | An DY,An, DY,Su, JG,et al. A Peptide-Coated Gold Nanocluster Exhibits Unique Behavior in Protein Activity Inhibition, A Peptide-Coated Gold Nanocluster Exhibits Unique Behavior in Protein Activity Inhibition[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,2015, 2015,137, 137(26):8412-8418, 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. |
入库方式： OAI收割
来源：高能物理研究所
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