It is well known that thiosalicylic acid and its S-alkyl derivatives have found applications in medicinal inorganic chemistry. Here are the study results on the interactions between the isobutyl derivatives of thiosalicylic acid (ligand, L) and human serum albumin (HSA). In particular, serum albumin is the primary soluble protein found in the human circulatory system. The metabolism of drugs, their distribution, and effectiveness strongly depend on the drug-albumin interaction. This interaction also affects the concentration of free drugs in the body. The interactions of the isobutyl derivatives of thiosalicylic acid (L) with HSA under physiological conditions was investigate by spectroscopy measurements and molecular docking. The results suggest that ligand could interact with HSA and influenced a slight change in the conformation of HSA through the static quenching mechanism. The analysis revealed that the HSA molecule has a moderate reaction to the ligand, as there is only one binding site for the ligand on the protein.