PlumX Metrics
Embed PlumX Metrics

Molecular simulation to aid in the understanding of the Aβ(1-42) peptide of Alzheimer's disease

Molecular Simulation, ISSN: 0892-7022, Vol: 26, Issue: 6, Page: 367-379
2001
  • 10
    Citations
  • 0
    Usage
  • 9
    Captures
  • 0
    Mentions
  • 0
    Social Media
Metric Options:   Counts1 Year3 Year

Metrics Details

  • Citations
    10
    • Citation Indexes
      10
  • Captures
    9

Article Description

The Aβ(1-42) peptide of Alzheimer's disease was studied by molecular modeling. The coordinates of the peptide were experimentally generated from solution-NMR spectroscopy, and the conformations were energy minimized using a combination of connectivity-based iterative partial equalization of orbital electronegativity with the MM + force field. There is a central folded domain in the Aβ peptide. This part is an apolar α-helix. The remaining residues form β-sheets. Aggregation requires that β-sheets interact by noncovalent bonding forces. The unsoluble, aggregated complexes are energetically stable and have ordered structures. A perspective in drug research is to design compounds that inhibit the hydrophobic cores of the individual Aβ peptides, blocking so the associations between the β-strains.

Bibliographic Details

Peter P. Mager; Robert Reinhardt; Katrin Fischer

Informa UK Limited

Chemistry; Computer Science; Mathematics; Chemical Engineering; Materials Science; Physics and Astronomy

Provide Feedback

Have ideas for a new metric? Would you like to see something else here?Let us know