Flow-induced dispersion analysis (FIDA) offers a rapid and cost-effective approach for screening and characterizing biomolecular binders. By measuring changes in the hydrodynamic radius of fluorescently labelled molecules and their complexes, FIDA enables direct detection of binding events in complex biological samples, such as heat-treated cell lysates, without immobilization. This allows identification of candidates with high affinity and stability in a single measurement, followed by quantitative affinity determination through titration. The low sample requirements and compatibility with crude preparations make FIDA a versatile tool for evaluating large sets of computational or experimentally generated binder designs.
Nowak et al. (Thu,) studied this question.