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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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P. G. Department of Studies in Chemistry, Karnatak University, Pavate Nagar, Dharwad-580 003, Karnataka India
Novel Drug Design and Discovery Laboratory, Department of Pharmaceutical Chemistry, S.E.T’s College of Pharmacy, Sangolli Rayanna Nagar, Dharwad 580 002, Karnataka, India
*Tel.: +91 9243995861. Fax: +91 836 274788. E-mail address: [email protected]
Cite this: Ind. Eng. Chem. Res. 2016, 55, 19, 5454–5464
Publication Date (Web):April 24, 2016
https://doi.org/10.1021/acs.iecr.6b00517
Copyright © 2016 American Chemical Society

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    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.

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    • Time-resolved fluorescence spectra for HSA (A) and HDL + HSA system and fluorescence spectra of HSA in the presence of β-cyclodextrin with varying concentration of Hydralazine (PDF)

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