Amyloid beta-peptide oligomerization in silico: dimer and trimer.
Soluble oligomers of Alzheimer's amyloid beta protein (Abeta) may act as effectors of neurotoxicity in early stages of Alzheimer's disease. Detailed information about the structure of Abeta in atomistic level and the dynamics of assembly of monomeric Abeta into oligomeric structures is rather elusive. We have performed replica exchange molecular dynamics (REMD) simulations on the formation of the dimer and trimer of Abeta10-35 peptide. We have observed spontaneous formation of several basic structural units that may act as a template or an intermediate for further aggregation of Alzheimer's Abeta protein. Various conformers, including interlocking structures of experimentally known bend double beta strands, are identified.
Jang
Soonmin
S
School of Chemistry, Seoul National University, Seoul 151-747, Korea.
Shin
Seokmin
S
D000544:Alzheimer Disease / Q000473:pathology; D016229:Amyloid beta-Peptides / Q000737:chemistry*; D003198:Computer Simulation; D019281:Dimerization; D009842:Oligopeptides / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry*; D011485:Protein Binding; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013696:Temperature; D013997:Time Factors
D016229:Amyloid beta-Peptides; D009842:Oligopeptides; D010446:Peptide Fragments