Spectroscopic and thermodynamic interaction studies of anti-diabetic drug with globular proteins

Drug-protein interaction is a fundamental problem in estimating the serious side effects of the drug. Hence, the main objective of this study was to study the interaction of acarbose with three different globular proteins i.e.; bovine serum albumin (BSA), human serum albumin (HSA), and hemoglobin (Hb) via UV-Visible absorption spectroscopic analysis. We were determined physicochemical parameters, binding constant, distribution constant and thermodynamic parameters activation energy, enthalpy, entropy, and Gibbs free energy by using UV-visible data. These both properties of acarbose-protein complexes indicated that the hydrogen bonding and weak van der Waals force played a major role in the interaction for complexation. The binding of acarbose with different proteins leads to change in the structure of protein folding which confirms by physicochemical and thermodynamic analysis.