Interaction of Hydralazine with Human Serum Albumin and Effect of β-Cyclodextrin on Binding: Insights from Spectroscopic and Molecular Docking Techniques

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Bolattin M, Nandibewoor S, Joshi S, Dixit S, Chimatadar S

Interaction of Hydralazine with Human Serum Albumin and Effect of β-Cyclodextrin on Binding: Insights from Spectroscopic and Molecular Docking Techniques

Industrial & Engineering Chemistry Research. 2016 Apr 24;55(19):5454-5464.

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Abstract

Biomolecular interaction of hydralazine with human serum albumin (HSA) was studied by fluorescence, ultravoilet, three-dimensional, synchronous, Fourier transform infrared, lifetime fluorescence, resonance Rayleigh scattering, circular dichroism, and molecular docking techniques. The intrinsic fluorescence of HSA was quenched by a static quenching mechanism. The effect of β-cyclodextrin on binding was studied. Binding constants and number of binding sites were evaluated using the Stern–Volmer equation. Thermodynamic parameters (ΔH°, ΔG°, and ΔS°) indicate the involvement of hydrogen bonding with weak van der Waals forces in the interaction. The average binding distance (r) between the HSA and hydralazine was calculated by Fourier resonance energy transfer theory. Molecular docking study confirms the drug binding sites and interaction of hydralazine with amino acid residues.

DrugBank Data that Cites this Article

Drugs

Hydralazine

Drug Carriers

Drug	Carrier	Kind	Organism	Pharmacological Action	Actions
Hydralazine	Serum albumin	Protein	Humans	Unknown	Binder	Details