液/固界面多肽分子组装精细结构的扫描隧道显微镜研究

doi:10.3866/PKU.WHXB20100440

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

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

Abstract

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

MAO Xiao-Bo, WANG Chen-Xuan, LIU Lei, MA Xiao-Jing, NIU Lin, YANG Yan-Lian, WANG Chen. Study on the Fine Structure of Polypeptides at Solid-Liquid Interfaces by Scanning Tunneling Microscopy[J].Acta Phys. -Chim. Sin., 2010, 26(04): 850-861.

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

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