In-Solution Characterization of Biomolecular Interaction Kinetics under Native Conditions.

ABSTRACT: Characterizing the kinetics of biomolecular interactions is fundamental for understanding biological mechanisms, developing novel drugs for advancing healthcare and for optimizing processes in protein engineering. Although modern surface-based methods have advanced our understanding of protein-protein and protein-ligand kinetics, they rely on immobilized samples, preventing the study of interactions under native conditions and leading to an incomplete understanding. In this work, we propose a paradigm shift by introducing a new method based on flow-induced dispersion analysis to study interaction kinetics while keeping biomolecules in solution, eliminating the need for surface immobilization and thereby preserving molecular mobility and avoiding structural constraints. The method examines

SUBMITTER: Willmer P 

PROVIDER: S-EPMC12444738 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature