Interaction of Lysozyme with Sulfated β-Cyclodextrin: Dissecting Salt and Hydration Contributions.

ABSTRACT: This article investigates the thermodynamic driving force of the interaction between lysozyme (Lys) and sulfated β-cyclodextrin (β-CDS), with a particular emphasis on the elusive role of hydration during polyelectrolyte-protein binding. Using isothermal titration calorimetry (ITC), the binding affinity was quantified across varying temperatures and salt concentrations, employing a recently developed thermodynamic framework that explicitly separates the contributions from counterion release and hydration effects. The study reveals that while counterion release is minimal in the Lys/β-CDS system, hydration effects become a dominant factor influencing the binding free energy ΔG_b, especially as experimental temperature deviates from the characteristic temperature T

SUBMITTER: Walkowiak JJ 

PROVIDER: S-EPMC12844233 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature