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Citation: 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 Physico-Chimica Sinica, ;2010, 26(04): 850-861. doi: 10.3866/PKU.WHXB20100440 shu

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

1.
National Center for Nanoscience and Technology, Beijing 100190, P. R. China

Received Date: 15 December 2009
Available Online: 10 March 2010

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.
- Self-assembly,
- Conformational disease,
- Amyloid protein,
- β-sheet,
- Scanning tunneling microscopy,
- Interface
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