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) |
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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