A mechanism for reversible mesoscopic aggregation in liquid solutions

TL;DR

This paper proposes a reversible aggregation mechanism in liquid solutions where transient binding stabilizes solute-rich inclusions, explaining mesoscopic clusters observed in protein solutions.

Contribution

It introduces a novel kinetic stabilization mechanism for reversible mesoscopic aggregation via transient molecular binding, extending understanding beyond traditional phase stability models.

Findings

Steady-state ensemble of inclusions can form outside traditional stability regions.

Transient binding causes kinetic stabilization of solute-rich droplets.

The mechanism explains observed mesoscopic clusters in protein solutions.

Abstract

We show systematically that a steady-state ensemble of mesoscopic inclusions of a solute-rich fluid can emerge in liquid solutions well outside the region of stability of the solute-rich phase. Unanticipated by conventional treatments, this type of reversible aggregation nonetheless can take place if the solute molecules bind transiently with each other to form long-lived complexes. The binding causes kinetic stabilization of inclusions of the solute-rich phase---within a substantial size range---so as to render the critical size for nucleation of the inclusions finite. Individual droplets nucleate and grow until they become mechanically unstable because of a concomitant drop in the internal pressure, the latter drop caused by the thermodynamic metastability of the solute-rich phase. At the same time, the {\em ensemble} of the droplets is steady-state on long times. In a freshly prepared solution, the ensemble is predicted to evolve similarly to the conventional Ostwald ripening, during which larger droplets grow at the expense of smaller droplets. The present mechanism is proposed to underlie the puzzling mesoscopic clusters observed in solutions of proteins and other molecules.