Abstract
AbstractThe assembly of amyloid peptides into highly organized fibrils is one of the major characteristics of many degenerative 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 correlation 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.
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