Insight into the interaction of benzothiazole tethered triazole analogues with human serum albumin: Spectroscopy and molecular docking approaches

Yadav, Priyanka; Yadav, Jitendra Kumar; Dixit, Arvind Kumar; Agarwal, Alka; Awasthi, Satish Kumar

doi:10.1002/bio.3676

Cited by 9 publications

(4 citation statements)

References 58 publications

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“…These two mechanisms can be differentiated by variation in the binding constant with varying temperatures and excited‐state lifetime. [ 43 ] To verify the quenching mode between BLC and NDP, the fluorescence quenching data were studied using following equations [ 44,45 ] :

\frac{F_{0}}{F} goodbreak= 1 goodbreak+ K_{SV} ([], Q)

\frac{F_{0}}{F} goodbreak= 1 goodbreak+ K_{q} τ_{0} ([], Q)

in which F and F 0 are the steady‐state fluorescence intensities of BLC with or without quencher, respectively. The quenching constant and concentration of NDP are represented by the K SV and [Q], respectively.…”

Section: Resultsmentioning

confidence: 99%

“…These two mechanisms can be differentiated by variation in the binding constant with varying temperatures and excited-state lifetime. [43] To verify the quenching mode between BLC and NDP, the fluorescence quenching data were studied using following equations [44,45] : respectively. τ 0 is the fluorescence lifetime of BLC free from quenching agent and K q is the quenching rate constant of the biomolecular form.…”

Section: Impacts Of Ndp On Blc Activitymentioning

confidence: 99%

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Elucidation on inhibition and binding mechanism of bovine liver catalase by nifedipine: multispectroscopic analysis and computer simulation methods

Zhou

Xiao

et al. 2022

Luminescence

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Nifedipine (NDP), a dihydropyridine calcium antagonist, is widely used for the treatment of hypertension and angina pectoris. Catalase is a key antioxidant enzyme that is closely relevant to the level of reactive oxygen specie in vivo. Here, the research explored the effects of NDP on the conformation and catalytic function of bovine liver catalase (BLC) through enzymatic reaction kinetic techniques, multispectroscopic analysis, and computer simulation methods. Kinetic studies clarified that the NDP reduced the activity of BLC using a noncompetitive inhibition mechanism.Based on trial data, a static quenching mechanism functioned in quenching the intrinsic fluorescence of BLC. The binding constant value was (4.486 ± 0.008) Â 10 4 M À1 (298 K) and BLC had one binding site for NDP. Tyr was prone to be exposed more to a hydrophilic environment in wake of a shift in fluorescence value. The binding reaction of BLC to NDP caused a conformational change in BLC, which in turn led to

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\frac{F_{0}}{F} goodbreak= 1 goodbreak+ K_{SV} ([], Q)

\frac{F_{0}}{F} goodbreak= 1 goodbreak+ K_{q} τ_{0} ([], Q)

Section: Resultsmentioning

confidence: 99%

Section: Impacts Of Ndp On Blc Activitymentioning

confidence: 99%

Elucidation on inhibition and binding mechanism of bovine liver catalase by nifedipine: multispectroscopic analysis and computer simulation methods

Zhou

Xiao

et al. 2022

Luminescence

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“…Active binding sites of serum albumins were recognized using MetaPocket server. Docking was performed by PatchDock server and Hex 8.0.0 Cuda, while docking complexes were visualized by Discovery Studio 3.0 and ligplot+ . The criteria for selection of the indicated structures were based on PDB advance BLAST analysis, and the structures used in this study were those displaying maximum score and query cover in BLAST.…”

Section: Methodsmentioning

confidence: 99%

Interaction of coumarin triazole analogs to serum albumins: Spectroscopic analysis and molecular docking studies

Sharma

Yadav

Sharma

et al. 2020

J of Molecular Recognition

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The interaction of triazole substituted 4-methyl-7-hydroxycoumarin derivatives (CUM1-4) with serum albumin (bovine serum albumin [BSA] and human serum albumin[HSA]) have been studied employing ultraviolet-visible (UV-Vis), fluorescence, circular dichroism (CD) spectroscopy, and molecular docking methods at physiological pH 7.4.The fluorescence quenching occurred with increasing concentration of CUMs, and the binding constant of CUM derivatives with BSA and HSA obtained from fluorescence quenching experiment was found to be~10 4 L mol −1 . CD study showed conformational changes in the secondary structure of serum albumin upon titration of CUMs.The observed experimental results were further validated by theoretical studies involving density functional theory (DFT) and molecular docking. K E Y W O R D S circular dichroism, coumarin, fluorescence quenching, molecular docking, serum albumin

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“…Human serum albumin (HSA) is the most copious and versatile carrier protein in the human body. It is a nonglycosylated polypeptide chain comprising 585 amino acids, with a molecular weight of 65 kDa and is responsible for the probable solubility of hydrophobic drugs in plasma . Serum albumin incorporates three homologous α-helical domains (I–III) which is further divided into two subdomains A and B.…”

Section: Introductionmentioning

confidence: 99%

Interaction between the Antimalarial Drug Dispiro-Tetraoxanes and Human Serum Albumin: A Combined Study with Spectroscopic Methods and Computational Studies

Yadav

Sharma

et al. 2020

ACS Omega

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Dispiro-tetraoxanes, a class of fully synthetic peroxides which can be used as an antiplasmodial remedy for multiple drug-resistant strains of Plasmodium falciparum, were selected for the interaction study with human serum albumin (HSA). The insight into the interaction of the two chemically synthesized, most potent antimalarial tetraoxane analogues (TO1 and TO2) and HSA has been scrutinized using distinct spectroscopic techniques such as. UV–visible absorption, fluorescence, time-resolved fluorescence, and circular dichroism (CD). Fluorescence quenching experiments divulged the static mode of quenching and binding constants obtained (∼104) indicated the moderate affinity of the analogues to HSA. CD confirmed the conformational changes in the serum albumin upon interaction with these analogues. Molecular docking validated the empirical results as these two analogues bind through hydrophobic interactions and hydrogen bonding with HSA. Present work first defined the binding mechanism of dispiro-tetraoxanes with HSA and thus provides a fresh insight into the drug transportation and metabolism. The present study could direct toward designing more potent tetraoxane analogues for their use in the biomedical field.

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Insight into the interaction of benzothiazole tethered triazole analogues with human serum albumin: Spectroscopy and molecular docking approaches

Cited by 9 publications

References 58 publications

Elucidation on inhibition and binding mechanism of bovine liver catalase by nifedipine: multispectroscopic analysis and computer simulation methods

Elucidation on inhibition and binding mechanism of bovine liver catalase by nifedipine: multispectroscopic analysis and computer simulation methods

Interaction of coumarin triazole analogs to serum albumins: Spectroscopic analysis and molecular docking studies

Interaction between the Antimalarial Drug Dispiro-Tetraoxanes and Human Serum Albumin: A Combined Study with Spectroscopic Methods and Computational Studies

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