Hydrophobic homopolymer's coil-globule transition and adsorption onto a hydrophobic surface under different conditions

TL;DR

This study uses Monte Carlo simulations to explore how a hydrophobic homopolymer undergoes coil-globule transitions and adsorbs onto hydrophobic surfaces, revealing the influence of confinement and water on these processes.

Contribution

It introduces a coarse-grained model incorporating water effects to analyze the response of hydrophobic homopolymers to environmental changes near interfaces.

Findings

Confinement enhances unfolding and adsorption of the polymer.

Hydration water modulates the coil-globule transition.

Polymer behavior depends on thermodynamic parameters.

Abstract

Unstructured proteins can modulate cellular responses to environmental conditions by undergoing coil-globule transitions and phase separation. However, the molecular mechanisms of these phenomena still need to be fully understood. Here, we use Monte Carlo calculations of a coarse-grained model incorporating water's effects on the system's free energy. Following previous studies, we model an unstructured protein as a polymer chain. Because we are interested in investigating how it responds to thermodynamic changes near a hydrophobic surface under different conditions, we choose an entirely hydrophobic sequence to maximize the interaction with the interface. We show that a slit pore confinement without top-down symmetry enhances the unfolding and adsorption of the chain in both random coil and globular states. Moreover, we demonstrate that the hydration water modulates this behavior depending on the thermodynamic parameters. Our findings provide insights into how homopolymers, and possibly unstructured proteins, can sense and adjust to external stimuli such as nanointerfaces or stresses.