Physicochemical characterisation of dihydro-alpha-lipoic acid interaction with human serum albumin by multi-spectroscopic and molecular modelling approaches

The binding of a popular food supplement and well-known antioxidant, dihydro-alpha-lipoic acid (DHLA) to human serum albumin (HSA) was characterised. monitored by several spectroscopic methods together with the molecular docking approach. HSA able bind DHLA moderate affinity, 1.00?0.05?104 M-1. Spectroscopic data demonstrated that preferential site for on is IIA (Sudlow I). Both experimental analysis identified electrostatic (salt bridges) hydrogen bonds as key interactions involved in HSA. Molecular confirmed Sudlow I could accommodate ligand bound protein specific conformation. dynamic simulation showed formed complex stable. Binding does not affect structure protein, but it thermally stabilises Bound had no effect susceptibility trypsin digestion. Since commonly used supplement, knowledge its pharmacokinetics pharmacodynamic properties an organism very important. This study further expands providing detailed interaction HSA, primary drug transporter circulation.