Amyloid beta (1-42) folding multiplicity and single-molecule binding behavior studied with STM

J Mol Biol. 2009 May 15;388(4):894-901. doi: 10.1016/j.jmb.2009.03.054. Epub 2009 Mar 25.

Abstract

The fine folding and assembling characteristics of amyloid beta (Abeta) peptides are important to pharmaceutical studies of drug molecules and to the pathological analysis of neurodegenerative disorders such as Alzheimer's disease at the molecular level. Here we present observations of the multiple folding characteristics of amyloid peptide Abeta(42) lamellae using scanning tunneling microscopy. Molecularly resolved core regions of Abeta(42) hairpins and unfolded peptide assembly structures are identified. The parallel assembling characteristics of Abeta(42) hairpins can be confirmed in the study. In addition, single-molecule binding characteristics of Congo red and thioflavin T have been shown to bind at the groove regions of peptide assemblies. This study demonstrates a complementary venue for studying molecular heterogeneity of peptide assemblies, as well as the binding characteristics of molecular modulators.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid beta-Peptides / chemistry*
  • Amyloid beta-Peptides / metabolism
  • Amyloid beta-Peptides / ultrastructure*
  • Benzothiazoles
  • Coloring Agents / chemistry
  • Coloring Agents / metabolism
  • Congo Red / chemistry
  • Congo Red / metabolism
  • Fluorescent Dyes / chemistry
  • Fluorescent Dyes / metabolism
  • Microscopy, Scanning Tunneling*
  • Molecular Structure
  • Peptide Fragments / chemistry*
  • Peptide Fragments / metabolism
  • Peptide Fragments / ultrastructure*
  • Protein Binding
  • Protein Conformation*
  • Protein Folding
  • Thiazoles / chemistry
  • Thiazoles / metabolism

Substances

  • Amyloid beta-Peptides
  • Benzothiazoles
  • Coloring Agents
  • Fluorescent Dyes
  • Peptide Fragments
  • Thiazoles
  • amyloid beta-protein (1-42)
  • thioflavin T
  • Congo Red