Initial Structural Models of the Aβ42 Dimer from Replica Exchange Molecular Dynamics Simulations.

ABSTRACT: Experimental characterization of the molecular structure of small amyloid (A)β oligomers that are currently considered as toxic agents in Alzheimer's disease is a formidably difficult task due to their transient nature and tendency to aggregate. Such structural information is of importance because it can help in developing diagnostics and an effective therapy for the disease. In this study, molecular simulations and protein-protein docking are employed to explore a possible connection between the structure of Aβ monomers and the properties of the intermonomer interface in the Aβ42 dimer. A structurally diverse ensemble of conformations of the monomer was sampled in microsecond timescale implicit solvent replica exchange molecular dynamics simulations. Representative structures with differe

SUBMITTER: Blinov N 

PROVIDER: S-EPMC6645216 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature