Structural and electronic analysis of the octarepeat region of prion protein with four Cu²⁺ by polarizable MD and QM/MM simulations.

ABSTRACT: Prions have been linked to neurodegenerative diseases that affect various species of mammals including humans. The prion protein, located mainly in neurons, is believed to play the role of metal ion transporter. High levels of copper ions have been related to structural changes. A 32-residue region of the N-terminal domain, known as octarepeat, can bind up to four copper ions. Different coordination modes have been observed and are strongly dependent on Cu²⁺ concentration. Many theoretical studies carried out so far have focused on studying the coordination modes of a single copper ion. In this work we investigate the octarepeat region coordinated with four copper ions. Molecular dynamics (MD) and hybrid quantum mechanics/molecular mechanics (QM/MM) simulations using the polariz

SUBMITTER: Nochebuena J 

PROVIDER: S-EPMC8497436 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature