Effects of familial mutations on the monomer structure of Aβ₄₂

Biophys J. 2012 Dec 19;103(12):L47-9. doi: 10.1016/j.bpj.2012.11.009. Epub 2012 Dec 18.


Amyloid beta (Aβ) peptide plays an important role in Alzheimer's disease. A number of mutations in the Aβ sequence lead to familial Alzheimer's disease, congophilic amyloid angiopathy, or hereditary cerebral hemorrhage with amyloid. Using molecular dynamics simulations of ∼200 μs for each system, we characterize and contrast the consequences of four pathogenic mutations (Italian, Dutch, Arctic, and Iowa) for the structural ensemble of the Aβ monomer. The four familial mutations are found to have distinct consequences for the monomer structure.

Publication types

  • Letter
  • Research Support, American Recovery and Reinvestment Act
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid beta-Peptides / chemistry*
  • Amyloid beta-Peptides / genetics*
  • Molecular Dynamics Simulation*
  • Mutation*
  • Peptide Fragments / chemistry*
  • Peptide Fragments / genetics*
  • Protein Structure, Secondary


  • Amyloid beta-Peptides
  • Peptide Fragments
  • amyloid beta-protein (1-42)