Protein migration via dissolution of ATP-stabilized condensate in a gradient of AMP

Abstract

We report the condensate-forming tendency of bovine serum albumin (BSA) increases in the presence of adenosine triphosphate (ATP) in macromolecularly crowded media. However, in the presence of adenosine monophosphate (AMP), the condensate does not form, and the ATP-stabilized condensate dissolves. Furthermore, we report protein migration and spatial tuning of BSA-mediated proton transfer catalysis towards an AMP gradient via the dissolution of ATP-stabilized condensates (dialytaxis). This dissolution-based functional protein mobility may have implications in active biocolloidal studies.