Early amyloid β-protein aggregation precedes conformational change

Chem Commun (Camb). 2014 May 25;50(40):5373-5. doi: 10.1039/c3cc48704k. Epub 2014 Jan 27.

Abstract

The aggregation of amyloid-β protein (1-42) is studied at experimental concentrations using all-atom molecular dynamics simulations. We observe a fast aggregation into oligomers without significant changes in the internal structure of individual proteins. The aggregation process is characterized in terms of transition networks.

MeSH terms

  • Amyloid beta-Peptides / chemistry*
  • Humans
  • Models, Molecular
  • Molecular Dynamics Simulation
  • Protein Binding
  • Protein Conformation*
  • Protein Multimerization*

Substances

  • Amyloid beta-Peptides