Glycopolymers stabilize protein folding and protein-protein interactions via enthalpic interactions.

ABSTRACT: Macromolecular crowding is ubiquitous in physiological environments, perturbing the thermodynamics and kinetics of proteins via excluded volume and nonspecific chemical interactions. While crowding has been well studied in vitro and in cells, the inert sugar polymers used to simulate crowding lack the chemical characteristics of biomolecules. Emerging studies guide the development of more relevant models of crowding in the cell, but little work has been done to discern crowding effects on proteins at the cell surface. Using ¹⁹F NMR, we measure how protein stability, folding, and intermolecular interactions are modulated by three glycopolymers abundant at the cellular exterior. Biologically relevant glycopolymers including heparin, hyaluronic acid, and mucin significantly stabili

SUBMITTER: Richter SM 

PROVIDER: S-EPMC12720779 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature