Site-specific Analysis of Amyloid Assemblies by Using Scanning Tunneling Microscopy  

作　　者：Yue Yu Yanlian Yang Chen Wang 

机构地区：[1]National Center for Nanoscience and Technology,Beijing 100190,China

出　　处：《Chinese Journal of Chemistry》2015年第1期24-34,共11页中国化学（英文版）

基　　金：supported by the National Natural Science Foundation of China (Nos.91127043,21273051,20911130229);the National Basic Research Program of China (Nos.2011CB932800,2009CB930100);the Chinese Academy of Sciences (No.KJCX2-YW-M15).

摘　　要：The assembly of amyloid peptides into highly organized fibrils is one of the major characteristics of many de-generative diseases such as Alzheimer’s disease and type II diabetes.Assembly structures of amyloid peptides at liquid-solid interface can be visualized by scanning tunneling microscopy(STM)with site-specific resolution.The STM analysis can provide valuable information on the folding mechanism of amyloid peptides based on the corre-lation of surface assembly structures and fibrillation behaviors.Cases on mutational analysis of amyloid peptides by STM are also reviewed which illustrate the capacities of STM studies on amyloid assemblies.

关 键 词：PEPTIDE AMYLOID ASSEMBLY scanning tunneling microscopy MUTATION 

分 类 号：R74[医药卫生—神经病学与精神病学]