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

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.

Interaction of Mitoxantrone-Loaded Cholesterol Modified Pullulan Nanoparticles with Human Serum Albumin and Effect on Drug Release

“…HSA contains a tryptophan that is excited in the ultraviolet region to emit fluorescence, forming a fluorescent spectrum. When other molecules interact with HSA, tryptophan fluorescence may change, depending on the effect of this interaction on protein conformation [27,28]. HSA and MTO, CHP NPs, and MTO-CHP NPs were mixed and reacted at a molecular ratio of 3.6 : 1 (HSA: 1 5 × 10 −5 mol/L).…”

“…The maximum changes in fluorescence intensity with recombination time were recorded. The tryptophan chromophore in the HSA molecule was excited at 280 nm [28], and the emission spectrum was recorded at 290-450 nm. The excitation and emission slit widths were 5 and 12 nm, respectively.…”

Luminescent sensing film based on sulfosalicylic acid modified Tb(III)-doped yttrium hydroxide nanosheets

“…Sample probes of equal volume but different concentrations were placed onto the sensor, and luminescence intensity changes were recorded using a fluorescence spectrometer. The relationship between the luminous intensity of the sensing film and CrO 4 2concentration was described by the Stern-Volmer equation, I 0 /I = 1 + K SV [CrO 4 2-] [19,20], where I 0 and I are luminescence intensities in the absence and presence of CrO 4 2-, respectively. The mechanism of CrO 4 2--induced luminescence quenching was studied using an Agilent Cary UV-8000 spectrophotometer (Timme, China).…”

The Cyclodextrin-Perfluorinated Surfactant Host-Guest Complex: Fundamental Studies for Potential Environmental Remediation and Therapeutic Applications

“…where C p is the molar concentration of the protein, n is the number of amino acid residues in the protein (585 for HSA), and l is the path length in mm. The MRE is then converted to the α-helical content by the following equation: where 4000 is the MRE of the β-form or random coil conformations at 208 nm, and 33000 is the MRE of a pure α-helical conformation at 208 nm (Bolattin et al 2016).…”

“…1.37 ± 1.07 × 10 3 -0.0126 ± 0.0017 0.942 Figure A33: Representative absorbance spectra of 10 μM HSA with no PFOA, 10 μM PFOA, and 100 μM PFOA. To correct for the inner filter effect, the following equation (Bolattin et al 2016) is used:…”