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

Abstract

Herein, we report that 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 ATP-stabilized condensate dissolves. Furthermore, we report protein migration and spatial tuning of BSA-mediated proton transfer catalysis towards AMP gradient via dissolution of ATP-stabilized condensates (dialytaxis). This dissolution-based protein mobility and heterogeneity in spatial functionality to gradients of adenosine nucleotides may find implications in active biocolloidal research.