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At 298 K, synchronous fluorescence spectrum of BSA with or without scoparone (a–f) were measured. The concentrations of scoparone differed from 0 to 1.65 × 10⁻⁵ mol L⁻¹ with a concentration gradient of 0.33 × 10⁻⁵ mol L⁻¹. CBSA = 1 × 10⁻⁵ mol L⁻¹, (A) Δλ = 15 nm, (B) Δλ = 60 nm
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Scoparone is a major biological active substance derived from the traditional Chinese herbal medicine called Artemisia capillaris. It has been confirmed that scoparone has anti-inflammatory, anti-tumor, hepatoprotective and antioxidant effects. However, the binding interaction of scoparone with bovine serum albumin (BSA) still remains unknown. Ther...
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... Several techniques are available to elucidate the mechanism of interaction of a drug with BSA. The most appropriate approach to understand and assess the fluorescence quenching and binding mechanism of EZT-BSA is the spectrofluorimetric method (Cao et al. 2018;Roy and Das 2016). BSA possesses intense fluorescence property due to the presence of Trp residues. ...
... With increase in the concentration of EZT, the α-helix of BSA increased gradually. Thus, it was evident that EZT induced the conformational changes in polypeptide chain of BSA (Cao et al. 2018). All these findings were supporting the results of synchronous fluorescence studies. ...
Biomolecular binding of a potential drug, ezetimibe (EZT) with bovine serum albumin (BSA) was investigated by spec-troscopic and electrochemical methods besides molecular modeling studies. Fluorescence measurements showed that the fluorescence intensity of BSA was quenched by EZT with a slight blue shift in the emission wavelength (from 346 to 340 nm). The values of binding constant, number of binding molecules and Stern-Volmer quenching constant of EZT-BSA system was calculated at different temperatures. The values of Stern-Volmer quenching constant increased with temperature indicating the presence of dynamic quenching mechanism. The probable location of EZT within the protein cavity (subdomain IIIA) was explored by docking studies and displacement experiments. Based on the values of free energy change, enthalpy change and entropy change, hydrophobic interaction was proposed to be the main factor that stabilized the EZT-BSA interaction. Studies on zeta potential of BSA unraveled the role of electrostatic interaction between EZT and BSA. In addition, synchronous fluorescence and circular dichroism spectral studies revealed the conformational changes occurred in BSA upon binding of EZT.
... Moreover, it also shows that CT/ECT quenches BSA intrinsic fluorescence through the static quenching mechanism, which promotes the creation of ground state complexes between BSA and CT/ECT [23]. This high magnitude of observed k q can be attributed to the process of complex formation via hydrophobic and hydrogen bond interaction between hydroxyl groups of CT/ECT and aromatic residues of BSA [63]. ...
... Further, the value of K a is in the order of 10 5 , confirming that there was an existence of strong interaction between CT/ECT and BSA. This interaction is probably the result of hydrophobic interaction between non-polar residues of BSA and CT/ECT, the possible hydrogen bond interaction between BSA and O-H groups at 3, 5, 7, 3 0 and 4 0 carbon position of CT/ECT [13,63]. ...
... The structure of BSA is made up of three homologous a-helical domains I, II and III, each domain is constituted by two subdomains A and B. The ligand binds to BSA at two major binding site namely sudlow site I and site II which are found at subdomain IIA and IIIA respectively [66]. The blind docking confirmed that the binding site is identified in subdomain II A at sudlow site I for BSA and CT interaction, and for BSA and ECT the binding site is seen at sudlow site II within subdomain IIIA [54,63]. The molecular docking conformations of BSA-CT and BSA-ECT with lowest binding energy are presented in the Fig. 4a and 4b respectively. ...
The interaction of two stereoisomeric flavanols (+) catechin (CT) and (-) epicatechin (ECT) with bovine serum albumin (BSA) has been studied using UV-Vis absorption and fluorescence spectroscopy. The binding affinity between flavanols and BSA is investigated through fluorescence quenching. Fluorescence study shows that both flavanols exhibit a strong interaction with BSA at a single binding site. This investigation indicates that CT/ECT may quench BSA fluorescence by the static quenching process due to the formation of ground state complex. The binding pocket of BSA is identified at the site I/II with the interaction of CT/ECT using molecular docking studies. Molecular dynamics simulation (MDS) reported the structural changes of BSA into sturdy α-helix formations owing to the interaction of CT/ECT. During the 200 ns simulation, BSA-ECT complex had lower root mean square deviation values, and undergoes slight structural deformations. The MDS result shows that the binding of CT/ECT with BSA is due to hydrophobic and hydrogen bond interactions, which supports the experimental outcomes. The analysis of radius of gyration confirmed that the BSA-ECT complex possessed a more compact structure. CT and ECT differ in their binding site and structural effects caused by distinct orientational positions at the benzopyran moiety. These findings help us to understand the binding nature of CT/ECT with BSA protein, and the effect of protein during blood transportation process.
... Synchronous fluorescence analysis. 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 3D spectroflurometric analysis. ...
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.
... 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 ∆ ° and ∆ ° [33]. Its positive enthalpy change (∆ °) also indicates the endothermic process of reaction [34]. ...
... 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]. ...
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.
Methyl chavicol (MC), also known as 1-methoxy-4-prop-2-enylbenzene, estragole or p-allylanisole, is a specific metabolite that can be found in the essential oils of both culinary and medicinal plants. It has antimicrobial, anti-inflammatory and insecticidal properties. In order to determine the binding mechanism and conformational changes of the in vitro interaction of MC with bovine serum albumin (BSA), several biophysical techniques as well as molecular modelling methods have been used. The fluorescence emission from BSA in the presence of MC at three distinctive temperatures was measured using 290 nm excitation wavelength. BSA's intrinsic fluorescence has been quenched by MC via a static process. The absorption peak shifts as a result of the development of the MC–BSA complex. Binding of MC with BSA caused conformational alterations, as seen by the fluorescence, UV–Vis absorption, circular dichroism and FTIR data. The values of the binding constants get increased as the temperature rises, indicating a stable complex formation under these conditions. Further, Site II, of BSA, has been discovered to have the strongest MC-binding affinity and hydrophobic interactions have been hypothesized to be the dominant interaction type in the BSA–MC complex because of the positive levels of enthalpy and entropy changes.
