Probing the Interaction Between Thioacetamide Fungicide and Bovine Serum Albumin Through Fluorescence, Electrochemical, and Docking Analyses

), with approximately one dominant binding site per BSA molecule. Thermodynamic analysis indicated a spontaneous process (ΔG < 0) with predominantly hydrophobic contributions. Synchronous and 3D fluorescence measurements showed pronounced microenvironmental changes around tryptophan residues, consistent with conformational rearrangements of BSA upon TAA binding. DLS further supported complex formation by showing an increase in the hydrodynamic diameter of BSA after TAA addition. DPV measurements exhibited a gradual decrease in the TAA oxidation current in the presence of BSA.