Reversible mesoscopic model of protein adsorption: From equilibrium to dynamics

TL;DR

This paper introduces a thermodynamically consistent mesoscopic model for protein adsorption at interfaces, capturing equilibrium properties and dynamics, and explaining non-monotonic behaviors observed experimentally.

Contribution

It develops a reversible mesoscopic model that unifies equilibrium and dynamic descriptions of protein adsorption, providing insights into non-trivial surface phenomena.

Findings

Predicts non-monotonic dependence of surface coverage on concentration

Reproduces experimental adsorption behaviors qualitatively

Offers a framework for studying protein exchange dynamics

Abstract

We present a thermodynamically consistent mesoscopic model of protein adsorption at liquid-solid interfaces. First describing the equilibrium state under varying protein concentration of the solution and binding conditions, we predict a non-trivial (non- monotonic) dependence of the experimentally observable properties of the adsorbed layer (such as the surface density and surface coverage) on these parameters. We subsequently proceed to develop a dynamical model consistent with the equilibrium description, which qualitatively reproduces known experimental phenomena and offers a promising way of studying the exchange of the adsorbed proteins by the proteins of the solution.