화학공학소재연구정보센터
Chemical Physics Letters, Vol.577, 131-137, 2013
Stable conformation of full-length amyloid-beta (1-42) monomer in water: Replica exchange molecular dynamics and ab initio molecular orbital simulations
Aggregation of amyloid beta-proteins (A beta) plays a key role in the mechanism of molecular pathogenesis of Alzheimer's disease (AD). It is known that full-length A beta(1-42) is more prone to aggregation than A beta(140). We here search stable conformations of solvated A beta(1-42) monomer by replica exchange molecular dynamics simulations based on classical force fields, and the most stable conformation is determined from the total energies evaluated by the ab initio fragment molecular orbital (FMO) calculations. In addition, based on the FMO results, the amino acid residues of A beta(1-42) contributing to the stabilization of the monomer are highlighted. (C) 2013 Elsevier B. V. All rights reserved.