Abstract
Fluorescence and circular dichroism spectroscopic techniques and molecular docking were used to study binding of azelastine with human serum albumin (HSA). Time resolve fluorescence spectroscopy results indicated that the quenching mechanism is dynamic. Fluorescence quenching results demonstrated that the binding of azelastine to HSA is weak, binding reaction is spontaneous. There is fluorescence energy transfer from tryptophan of HSA to bound azelastine. 2.34 nm is the binding distance calculated from FRET data. Molecular docking results suggested that the binding site for azelastine in HSA is located in subdomain II A. Interaction of azelastine to HSA induced ordered secondary structure in HSA. Binding of azelastine to HSA can affect pharmacokinetics of drug. Hence, rationalizing drug dosage is important for clinical application of azelastine.
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•The binding interaction between azelastine and human serum albumin is weak.•Azelastine caused fluorescence quenching of human serum albumin.•Azelastine interacts with HSA in dynamic mode.•Azelastine binds to domain II on HSA molecule.•Binding of azelastine induced ordered secondary structure in HSA.