Study of the binding interactions between uric acid and bovine serum albumin using multiple spectroscopic techniques

Makarska-Białokoz, Magdalena; Lipke, Agnieszka

doi:10.1016/j.molliq.2018.12.026

Cited by 70 publications

(20 citation statements)

References 80 publications

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“…Next, donor and quencher have to be situated in a close proximity to one another within 2-8 nm. Lastly, the orientations of transition dipole of the acceptor and donor must be aligned to each other [35]. FRET is an advantageous method for measuring the distance between quencher and fluorophore, which helps distinguish whether ligand binds to protein in the close proximity with Trp residues.…”

Section: Fluorescence Resonance Energy Transfer (Fret) Investigationmentioning

confidence: 99%

Insight into the Molecular Interaction of Cloxyquin (5-chloro-8-hydroxyquinoline) with Bovine Serum Albumin: Biophysical Analysis and Computational Simulation

Phopin

Ruankham

Prachayasittikul

et al. 2019

IJMS

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Cloxyquin is a potential therapeutic compound possessing various bioactivities, especially antibacterial, antifungal, cardioprotective, and pain relief activities. Herein, the interaction mechanism between cloxyquin and bovine serum albumin (BSA) has been elucidated in order to fulfill its pharmacokinetic and pharmacodynamic gaps essential for further development as a therapeutic drug. Multi-spectroscopic and biophysical model analysis suggested that cloxyquin interacts with BSA via a static process by ground-state complex formation. Its binding behavior emerged as a biphasic fashion with a moderate binding constant at the level of 104 M−1. Thermodynamic analysis and molecular docking simulation concurrently revealed that hydrophobic interaction is a major driving force for BSA–cloxyquin complexation. Binding of cloxyquin tends to slightly enlarge the monomeric size of BSA without a significant increase of aggregate fraction. Cloxyquin preferentially binds into the fatty acid binding site 5 (FA5) of the BSA via hydrophobic interaction amongst its quinoline scaffold and Phe550, Leu531, and Leu574 residues of BSA. The quinoline ring and hydroxyl moiety of cloxyquin also form the π–π interaction and the hydrogen bond with Phe506. Our data indicate a potential function of serum albumin as a carrier of cloxyquin in blood circulation.

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Section: Fluorescence Resonance Energy Transfer (Fret) Investigationmentioning

confidence: 99%

Insight into the Molecular Interaction of Cloxyquin (5-chloro-8-hydroxyquinoline) with Bovine Serum Albumin: Biophysical Analysis and Computational Simulation

Phopin

Ruankham

Prachayasittikul

et al. 2019

IJMS

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“…Based on the meaning of physical quantities in equations – and our practical experimental conditions, the values 2/3, 1.336 and 0.118 could be adopted for the K 2 , N , and ф , respectively . Finally, characteristic parameters in equations were calculated to be: J = 5.866 × 10 −18 L mol −1 cm 3 , R 0 = 0.71 nm, E = 0.01 and r = 1.53 nm.…”

Section: Resultsmentioning

confidence: 99%

Spectroscopic and computational exploration of hypoxanthine riboside interacting with plasma albumin

2019

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Hypoxanthine riboside (HXR) is a nucleoside essential for wobble base pairs to translate the genetic code. In this work, an absorption and luminescence study showed that HXR and human serum albumin (HSA) formed a new complex through hydrogen bonds and van der Waals forces at ground state. Fluorescence probe experiments indicated that HXR entered the first subdomain of domain II in HSA and was fixed by amino acid residues in site I defined by Sudlow, and after competing with a known site marker. The recognition interaction featured negative ΔH ϴ , ΔS ϴ and ΔG ϴ thermodynamic parameters. Fluorescence and circular dichroism spectra described the polarity of residues and α-helix and β-strand content changed because of HXR binding. The most rational structure for the HXR-HSA complex was recommended by the molecular docking method, in which the binding location, molecular orientation, adjacent amino acid residues, and hydrogen bonds were included. In addition, the influence of β-cyclodextrin and some essential metal ions on the balance of the HSA-HXR system interaction was measured. The study gained comprehensive information on the transportation mechanism for HXR in blood, and was of great significance in understanding the theory of HXR biotransformation and in discussing its clinical in vivo half-life.

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“…The Stern-Volmer plots were found to be linear within the studied concentration range which enunciates either a single type of quenching or the presence of only a single binding site for a quencher 55,59,60 . The Stern-Volmer plots for aqueous medium exhibit slightly upward curvature at higher quencher concentrations which reveals the presence of mixed quenching i.e., both static and dynamic 61,62 . The results display that the value of K q is two orders of magnitude for both systems in water and urea solution more than the maximum diffusion collision quenching rate constant 2.0 10 10 Lmol 1 s 1 for different quenchers with biopolymer 53 .…”

Section: Binding Behavior Study Between Bsa and Cfhmentioning

confidence: 97%

Effect of Temperature and Additives on the Interaction of Ciprofloxacin Hydrochloride Drug with Polyvinylpyrrolidone and Bovine Serum Albumin: Spectroscopic and Molecular Docking Study

et al. 2021

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The fluoroquinolone antibiotic drug namely ciprofloxacin hydrochloride (CFH) is widely prescribed for the treatment of different bacterial infections. The interaction of CFH with a synthetic polymer, polyvinyl pyrrolidone (PVP), and biopolymer, bovine serum albumin (BSA) was studied by UVvisible and fluorescence spectroscopic methods at different temperatures. The binding constant (K b ) for the CFH-PVP complex was determined from the Benesi-Hildebrand plot. PVP of different molecular weights (MW) (such as 24,000, 40,000, 360,000, and 700,000 gm. mole -1 ) were used for the interaction between CFH and PVP. There was a gradual increase in K b value and the complexation reaction was found to be much enhanced with the augmentation of the MW of PVP. The values of K b were also found to be increased with increasing temperatures as well as with the increase of electrolyte/acetic acid concentration. The Gibbs free energy of binding (∆G 0 ) values of the interaction process was negative which indicates the complex formation is thermodynamically spontaneous. The positive values of enthalpy (∆H 0 ) and entropy (∆S 0 ) of binding connote that the binding force for CFH-PVP complexation is hydrophobic in nature and the complexation is entropy controlled. The negative intrinsic enthalpy (∆H *,0 ) values indicate the high stability of CFH-PVP complexes. Molecular docking calculation discloses the existence of similar binding forces between CFH and PVP obtained by the analysis of experimental data from UV-visible spectroscopic method. The binding constant between CFH and BSA (K b ), quenching constant (K sv ), the number of binding sites (n), and the quenching rate constant (K q ) for the CFH-BSA system were also calculated. The values of K sv , K q , and n for the CFH-BSA system are lower in 0.05 mol kg -1 urea solution and higher in PVP solutions compared to those of aqueous medium.

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Study of the binding interactions between uric acid and bovine serum albumin using multiple spectroscopic techniques

Cited by 70 publications

References 80 publications

Insight into the Molecular Interaction of Cloxyquin (5-chloro-8-hydroxyquinoline) with Bovine Serum Albumin: Biophysical Analysis and Computational Simulation

Insight into the Molecular Interaction of Cloxyquin (5-chloro-8-hydroxyquinoline) with Bovine Serum Albumin: Biophysical Analysis and Computational Simulation

Spectroscopic and computational exploration of hypoxanthine riboside interacting with plasma albumin

Effect of Temperature and Additives on the Interaction of Ciprofloxacin Hydrochloride Drug with Polyvinylpyrrolidone and Bovine Serum Albumin: Spectroscopic and Molecular Docking Study

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