Characterization of interaction between scoparone and bovine serum albumin: spectroscopic and molecular docking methods

Cao, Xiangyu; He, Yonglin; Liú, Dan; Yin, He; Hou, Xin; Cheng, Ye; Liu, Jianli

doi:10.1039/c8ra04065f

Cited by 43 publications

(15 citation statements)

References 33 publications

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“…The BSA-cloxyquin complex is more likely to occur at lower cloxyquin concentrations as indicated by its~2.5 times lesser binding energy than those of higher concentrations. Additionally, the hydrophobic forces mainly drive the interaction of cloxyquin and BSA owing to the positive values of both ∆H • and ∆S • [33]. Its positive enthalpy change (∆H • ) also indicates the endothermic process of reaction [34].…”

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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“…Further, the interaction between BSA and MiADMSA was investigated using synchronous fluorescence spectroscopy 21 , 39 . The study is helpful to understand the change in the microenvironment of fluorophore residues mainly Tyr and Trp residues of BSA 40 .…”

Section: Resultsmentioning

confidence: 99%

Interaction study of monoisoamyl dimercaptosuccinic acid with bovine serum albumin using biophysical and molecular docking approaches

Thakur

Patwa

Pant

et al. 2021

Sci Rep

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Monoisoamyl 2,3-dimercaptosuccinic acid (MiADMSA), a lipophilic chelator has been evaluated for its potential use as an antidote in arsenic poisoning. The pharmacokinetics and pharmacodynamics properties of a drug could be understood via study its mechanism of interaction with bovine serum albumin protein (BSA). Therefore, the interaction between MiADMSA with BSA was investigated using various spectroscopic techniques and computational methods. Linear quenching of BSA intrinsic fluorescence intensity with the increasing concentration of MiADMSA was observed in the fluorescence study. Furthermore, synchronous results revealed that MiADMSA slightly changed the conformation of BSA. The binding constant value of the BSA-MiADMSA complex was found 1.60 × 104 M−1 at 298 K. The value of thermodynamic parameters ΔG, ΔH, and ΔS described that the process is spontaneous, endothermic, and hydrophobic forces are involved in the interaction of MiADMSA with BSA. Competitive site marker experiments showed that MiADMSA binds to site-II of BSA. Conformational changes of BSA with the interaction of MiADMSA were apparent by CD, UV–Visible, FT-IR, and 3D fluorescence spectroscopy. To strengthen the experimental findings we have also performed a theoretical study on the BSA-MiADMSA complex. Two sites were identified with docking score of − 6.642 kcal/mol at site IIa and − 3.80 kcal/mol for site IIb via molecular docking study. Molecular dynamics simulation study inferred the stability of the BSA-MiADMSA complex which was analyzed in a long simulation run. The experimental and computational studies have shown the effective binding of MiADMSA with BSA which is essential for the transportation and elimination of a drug from the body.

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“…UV-vis absorbance UV-visible absorption spectroscopy is a widely employed technique to detect the conformational changes occurring due to drug-protein interactions. 26 HSA exhibited an absorption peak at 280 nm due to the p-p* transitions of Trp, Tyr and Phe amino acids. 27 The interaction of CTs and HSA was evaluated by recording the spectra of the protein in the absence and presence of various concentrations of CTs.…”

Section: Resultsmentioning

confidence: 99%

“…38 The k q values were calculated assuming the s o value to be 10 À8 s. Furthermore, the value of the quenching rate constant at all the temperatures was found to be much greater than the maximum diffusion rate constant of a biomolecule, i.e., 2 Â 10 10 M s À1 ( Table 1), suggesting that the uorescence quenching of HSA by CTs led to the formation of a static complex. 26 Further uorescence data were analysed to determine the binding sites by using the modied Stern-Volmer equation: 39…”

Section: Analysis Of Uorescence Quenchingmentioning

confidence: 99%

Insights into the interaction of potent antimicrobial chalcone triazole analogs with human serum albumin: spectroscopy and molecular docking approaches

Yadav

Agarwal

et al. 2019

RSC Adv.

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Characterization of interaction between scoparone and bovine serum albumin: spectroscopic and molecular docking methods

Abstract: The interaction of scoparone with bovine serum albumin (BSA) was studied by utilizing spectroscopic and molecular docking methodologies.

Cited by 43 publications

References 33 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

Interaction study of monoisoamyl dimercaptosuccinic acid with bovine serum albumin using biophysical and molecular docking approaches

Insights into the interaction of potent antimicrobial chalcone triazole analogs with human serum albumin: spectroscopy and molecular docking approaches

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