Amyloid-beta(29-42) dimer formations studied by a multicanonical-multioverlap molecular dynamics simulation.
Amyloid-beta peptides are known to form amyloid fibrils and are considered to play an important role in Alzheimer's disease. Amyloid-beta(29-42) is a fragment of the amyloid-beta peptide and also has a tendency to form amyloid fibrils. In order to study the mechanism of amyloidogenesis of this fragment, we applied one of the generalized-ensemble algorithms, the multicanonical-multioverlap algorithm, to amyloid-beta(29-42) dimer in aqueous solution. We obtained a detailed free-energy landscape of the dimer system. From the detailed free-energy landscape, we examined monomer and dimer formations of amyloid-beta(29-42) and deduced dimerization processes, which correspond to seeding processes in the amyloidogenesis of amyloid-beta(29-42).
Itoh
Satoru G
SG
Department of Physics, School of Science, Nagoya University, Nagoya, Aichi, Japan. itoh@tb.phys.nagoya-u.ac.jp
Okamoto
Yuko
Y
D016229:Amyloid beta-Peptides / Q000737:chemistry*; D003198:Computer Simulation; D019281:Dimerization; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry*; D020836:Protein Structure, Quaternary
D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C512364:beta-amyloid peptide (29-42)