Atomistic simulation of the Coupled adsorption and unfolding of protein GB1 on the polystyrenes nanoparticle surface

TL;DR

This study uses atomistic molecular dynamics simulations with metadynamics to explore how the protein GB1 adsorbs and unfolds on a polystyrene nanoparticle surface, revealing detailed conformational and interaction dynamics.

Contribution

It provides the first atomistic simulation-based detailed view of coupled protein adsorption and unfolding on nanoparticle surfaces, introducing a new comprehensive scenario.

Findings

Identified three distinct protein states involving adsorption and desorption.

Analyzed changes in GB1's secondary and tertiary structures during adsorption.

Elucidated dominant interactions at different stages of adsorption.

Abstract

Protein adsorption/desorption upon nanoparticle surfaces is an important process to understand for developing new nanotechnology involving biomaterials, while atomistic picture of the process and its coupling with protein conformational change is lacking. Here we report our study on the adsorption of protein GB1 upon a polystyrene nanoparticle surface using atomistic molecular dynamic simulations. Enabled by metadynamics, we explored the relevant phase space and identified three protein states; each protein state involved both the adsorbed and desorbed states. We also studied the change of secondary and tertiary structures of GB1 during adsorption, and the dominant interactions between protein and surface in different adsorbing stages. From the simulation results we obtained a scenario that is more rational and complete than the conventional one. We believe the new scenario is more appropriate as a theoretical model in understanding and explaining experimental signals. Introduction