物理化学学报 >> 2010, Vol. 26 >> Issue (04): 850-861.doi: 10.3866/PKU.WHXB20100440

胶体及界面化学 上一篇    下一篇

液/固界面多肽分子组装精细结构的扫描隧道显微镜研究

毛晓波, 王晨轩, 刘磊, 马晓晶, 牛琳, 杨延莲, 王琛   

  1. 国家纳米科学中心, 北京 100190
  • 收稿日期:2009-12-15 修回日期:2010-03-03 发布日期:2010-04-02
  • 通讯作者: 王琛 E-mail:wangch@nanoctr.cn

Study on the Fine Structure of Polypeptides at Solid-Liquid Interfaces by Scanning Tunneling Microscopy

MAO Xiao-Bo, WANG Chen-Xuan, LIU Lei, MA Xiao-Jing, NIU Lin, YANG Yan-Lian, WANG Chen   

  1. National Center for Nanoscience and Technology, Beijing 100190, P. R. China
  • Received:2009-12-15 Revised:2010-03-03 Published:2010-04-02
  • Contact: WANG Chen E-mail:wangch@nanoctr.cn

摘要:

介绍了与蛋白构象病相关的淀粉样多肽分子组装结构的研究进展. 综述了在固体、溶液以及界面等不同状态下多肽分子组装结构的表征方法, 对于扫描隧道显微技术(STM)在解析多肽分子界面组装结构方面的研究进展进行了重点评述, 主要包括在液/固界面上的多肽分子组装结构的精细特征, 界面诱导的多肽构象转变, 调节分子、染料等与多肽组装结构的相互作用模式和位点识别等.

关键词: 自组装, 构象病, 淀粉样蛋白, β-片层结构, 扫描隧道显微技术, 界面

Abstract:

In this review, a summary of recent research progress on the assembly structures of amyloid peptides related to protein conformational diseases is presented. Various characterization methods have been introduced to study the peptide assembly structures in solid-state, in solution, and at interfaces. Recent work on the structural analysis of peptide assemblies at solid-liquid interfaces has been undertaken using scanning tunneling microscopy, and these include the determination of the fine structures of peptide as-semblies at solid/liquid interfaces, surface-induced protein conformational changes and interactions between peptides and modulator or labeling molecules.

Key words: Self-assembly, Conformational disease, Amyloid protein, β-sheet, Scanning tunneling microscopy, Interface

MSC2000: 

  • O647