Acta Phys. -Chim. Sin. ›› 2010, Vol. 26 ›› Issue (04): 850-861.doi: 10.3866/PKU.WHXB20100440

• COLLOID AND INTERFACE CHEMISTRY • Previous Articles     Next Articles

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


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


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