Study on the fine structure of polypeptides at solid-liquid interfaces by scanning tunneling microscopy

Xiao Bo Mao; Chen Xuan Wang; Lei Liu; Xiao Jing Ma; Lin Niu; Yan Lian Yang; Chen Wang

Study on the fine structure of polypeptides at solid-liquid interfaces by scanning tunneling microscopy

Xiao Bo Mao, Chen Xuan Wang, Lei Liu, Xiao Jing Ma, Lin Niu, Yan Lian Yang, Chen Wang

School of Medicine

Research output: Contribution to journal › Review article › peer-review

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 assemblies at solid/liquid interfaces, surface-induced protein conformational changes and interactions between peptides and modulator or labeling molecules.

Original language	English (US)
Pages (from-to)	850-861
Number of pages	12
Journal	Wuli Huaxue Xuebao/ Acta Physico - Chimica Sinica
Volume	26
Issue number	4
State	Published - Apr 2010

Keywords

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

ASJC Scopus subject areas

Physical and Theoretical Chemistry

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title = "Study on the fine structure of polypeptides at solid-liquid interfaces by scanning tunneling microscopy",

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 assemblies at solid/liquid interfaces, surface-induced protein conformational changes and interactions between peptides and modulator or labeling molecules.",

keywords = "Amyloid protein, Conformational disease, Interface, Scanning tunneling microscopy, Self-assembly, β-sheet",

author = "Mao, {Xiao Bo} and Wang, {Chen Xuan} and Lei Liu and Ma, {Xiao Jing} and Lin Niu and Yang, {Yan Lian} and Chen Wang",

year = "2010",

month = apr,

language = "English (US)",

volume = "26",

pages = "850--861",

journal = "Acta Physico - Chimica Sinica",

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publisher = "Beijing University Press",

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T1 - Study on the fine structure of polypeptides at solid-liquid interfaces by scanning tunneling microscopy

AU - Mao, Xiao Bo

AU - Wang, Chen Xuan

AU - Liu, Lei

AU - Ma, Xiao Jing

AU - Niu, Lin

AU - Yang, Yan Lian

AU - Wang, Chen

PY - 2010/4

Y1 - 2010/4

N2 - 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 assemblies at solid/liquid interfaces, surface-induced protein conformational changes and interactions between peptides and modulator or labeling molecules.

AB - 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 assemblies at solid/liquid interfaces, surface-induced protein conformational changes and interactions between peptides and modulator or labeling molecules.

KW - Amyloid protein

KW - Conformational disease

KW - Interface

KW - Scanning tunneling microscopy

KW - Self-assembly

KW - β-sheet

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M3 - Review article

AN - SCOPUS:77950349264

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SP - 850

EP - 861

JO - Acta Physico - Chimica Sinica

JF - Acta Physico - Chimica Sinica

SN - 1000-6818

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