The dissolution of silver nanoparticles (AgNPs) to release Ag(I)(aq) is an important mechanism in potentiating AgNP cytotoxicity and imparting their antibacterial properties. However, AgNPs can undergo other simultaneous biophysicochemical transformations, such as protein adsorption, which can mediate AgNP dissolution behaviors. We report the comprehensive analysis of AgNP dissolution and protein adsorption behaviors with monolayer surface coverage of AgNPs by bovine serum albumin (BSA). AgNP dissolution rate constants, , were quantified over several particle sizes (10, 20, and 40 nm) and BSA concentrations (0-2 nM) using linear sweep stripping voltammetry. Across all particle sizes, the dissolution rate constant increased with increasing BSA concentrations. However, protein-enhanced dissolution behaviors were most pronounced for 10 nm AgNPs, which exhibited 3.6-fold and 7.7-fold relative enhancement when compared to 20 and 40 nm AgNPs, respectively. Changes to AgNP surface properties upon interaction with BSA were monitored using dynamic light scattering and zeta potential measurements, while BSA-AgNP complex formation was evaluated using UV-vis spectroscopy and circular dichroism spectroscopy. A subtle increase in the BSA-AgNP association constant was observed with an increase in the AgNP size. Together, these results suggest that the AgNP size dependence of BSA-enhanced dissolution of AgNPs is possibly mediated through both displacement of Ag(I)(aq)-loaded BSA by excess protein in the bulk solution and minimized accessibility of the AgNP surface because of BSA adsorption.