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 |
| Externally published | Yes |
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Keywords
- β-sheet
- Amyloid protein
- Conformational disease
- Interface
- Scanning tunneling microscopy
- Self-assembly
ASJC Scopus subject areas
- Physical and Theoretical Chemistry
Cite this
Study on the fine structure of polypeptides at solid-liquid interfaces by scanning tunneling microscopy. / Mao, Xiaobo; Wang, Chen Xuan; Liu, Lei; Ma, Xiao Jing; Niu, Lin; Yang, Yan Lian; Wang, Chen.
In: Wuli Huaxue Xuebao/ Acta Physico - Chimica Sinica, Vol. 26, No. 4, 04.2010, p. 850-861.Research output: Contribution to journal › Review article
}
TY - JOUR
T1 - Study on the fine structure of polypeptides at solid-liquid interfaces by scanning tunneling microscopy
AU - Mao, Xiaobo
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 - β-sheet
KW - Amyloid protein
KW - Conformational disease
KW - Interface
KW - Scanning tunneling microscopy
KW - Self-assembly
UR - http://www.scopus.com/inward/record.url?scp=77950349264&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77950349264&partnerID=8YFLogxK
M3 - Review article
AN - SCOPUS:77950349264
VL - 26
SP - 850
EP - 861
JO - Acta Physico - Chimica Sinica
JF - Acta Physico - Chimica Sinica
SN - 1000-6818
IS - 4
ER -