Replica exchange molecular dynamics simulation of the coordination of Pt(ii)-Phenanthroline to amyloid-β.

ABSTRACT: We report replica exchange molecular dynamics (REMD) simulations of the complex formed between amyloid-β peptides and platinum bound to a phenanthroline ligand, Pt(phen). After construction of an AMBER-style forcefield for the Pt complex, REMD simulation employing temperatures between 270 and 615 K was used to provide thorough sampling of the conformational freedom available to the peptide. We find that the full length peptide Aβ42, in particular, frequently adopts a compact conformation with a large proportion of α- and 3,10-helix content, with smaller amounts of β-strand in the C-terminal region of the peptide. Helical structures are more prevalent than in the metal-free peptide, while turn and strand conformations are markedly less common. Non-covalent interactions, including salt-bridg

SUBMITTER: Turner M 

PROVIDER: S-EPMC9074135 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature