Abstract

Aggregation of proteins is a serious problem, affecting both industrial production of proteins and human health. Despite recent advances in the theories and experimental techniques available to address understanding of protein aggregation processes, mechanisms of aggregate formation have proved challenging to study. This is in part because the typical irreversibility of protein aggregation processes at atmospheric conditions complicates analysis of their kinetics and thermodynamics. Because high hydrostatic pressures act to disfavor the hydrophobic and electrostatic interactions that cause protein aggregation, studies conducted under high hydrostatic pressures may allow protein aggregates to be formed reversibly, enabling thermodynamic and kinetic parameters to be measured in greater detail. Although application of high hydrostatic pressures to protein aggregation problems is rather recent, a growing literature, reviewed herein, suggests that high pressure may be a useful tool for both understanding protein aggregation and reversing it in industrial applications.