Electronic Polarizability Tunes the Function of the Human Bestrophin 1 Cl^- Channel.

ABSTRACT: Mechanisms of anion permeation within ion channels and nanopores remain poorly understood. Recent cryo-electron microscopy structures of the human bestrophin 1 Cl- channel (hBest1) provide an opportunity to evaluate ion interactions predicted by molecular dynamics (MD) simulations against experimental observations. Here, we implement the fully polarizable forcefield AMOEBA in MD simulations on different conformations of hBest1. This forcefield models multipole moments up to the quadrupole; therefore, it captures induced dipole and anion-π interactions. We show that key biophysical properties of the channel can only be simulated when electronic polarization is included in the molecular models and that Cl- permeation through the neck of the pore is achieved through hydrophobic solvation conc

SUBMITTER: Phan LX 

PROVIDER: S-EPMC10680768 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature