Effect of N‐Butyl‐N‐Methyl‐Morpholinium Bromide Ionic Liquid on the Conformation Stability of Human Serum Albumin

Kumari, Meena; Singh, Upendra Kumar; Singh, Prashant; Patel, Rajan

doi:10.1002/slct.201601477

Cited by 56 publications

(32 citation statements)

References 82 publications

(109 reference statements)

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“…First tiny peak (Peak I) mainly represented the Raleigh scattering . Two strong fluorescence peaks could be seen, peak II and peak III in Figure , where peak II was observed due to the π‐π* transition of the polypeptide backbone of BSA, while peak III stands for tryptophan and tyrosine residues . The intensity of peak II decreased rapidly from 786 to 702 with simultaneous decrease in stoke shift indicating disturbance of the polypeptide backbone structure of BSA after binding with 4MMC.…”

Section: Resultsmentioning

confidence: 95%

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Esterase activity and conformational changes of bovine serum albumin toward interaction with mephedrone: Spectroscopic and computational studies

Patel

Maurya

Parray

et al. 2018

J of Molecular Recognition

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The present work is a brief overview of the effect of psychostimulant drug mephedrone hydrochloride (4MMC) on a transport protein, bovine serum albumin (BSA). The binding effect of 4MMC on BSA has been investigated by using UV-visible, steady-state fluorescence, time-resolved fluorescence, fluorescence resonance energy transfer, Fourier transform infrared, circular dichroism, and molecular docking method. 4-Methylmephedrone quenched the intrinsic fluorescence of BSA by static quenching mechanism, which was further confirmed by time-resolved fluorescence. The absorption spectrum of BSA in the presence of various concentrations of 4MMC reveals the change in the absorption bands of BSA-4MMC complex. The binding constant between 4MMC and BSA was calculated to be of the order of 10 Lmol . The thermodynamic parameters such as molar enthalpy change (∆H), molar Gibbs free energy change (∆G), and molar entropy contribution (∆S) were obtained by the van't Hoff equation. The values obtained suggested that the binding mechanism was entropic driven and the major forces involved are hydrophobic in nature. The fluorescence resonance energy transfer result indicates the high probability of energy transfer from Trp residue of BSA to the 4MMC (r = 2.01 nm). Fourier transform infrared and CD results showed that 4MMC induced secondary structural changes in BSA. The esterase-like activity of BSA in presence of 4MMC further validated our CD results, confirming the distortion and change in functionality of protein upon binding with 4MMC. Molecular docking analysis showed that 4MMC principally bind at the II site (subdomain IIIA) of BSA.

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Section: Resultsmentioning

confidence: 95%

“…Synchronous fluorescence spectra were acquired by the same spectrofluorometer at 298 K. The difference between excitation and the emission wavelength was kept constant (Δ λ = λ em − λ ex ). The 3D fluorescence was also recorded on the same instrument by setting the excitation at 200 nm and with an increment of 10 nm …”

Section: Methodsmentioning

confidence: 99%

Esterase activity and conformational changes of bovine serum albumin toward interaction with mephedrone: Spectroscopic and computational studies

Patel

Maurya

Parray

et al. 2018

J of Molecular Recognition

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“…The fluorescence spectrum of protein is highly sensitive to the polarity of the microenvironment of the fluorophore residues. Therefore, fluorescence spectroscopy has been widely used for monitoring the conformational changes in the protein induced by ligand binding . Shift in emission wavelength and change in fluorescence intensity which are mainly attributed with the alteration in position of intrinsic fluorophores were utilized for analysis of TTH–BSA interaction.…”

Section: Resultsmentioning

confidence: 99%

Effect of triazole‐tryptophan hybrid on the conformation stability of bovine serum albumin

et al. 2018

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The effect of a potent antimicrobial compound bearing 1,2,3-triazole core and a tryptophan tail, triazole-tryptophan hybrid (TTH), with bovine serum albumin (BSA) have been explored using various spectroscopic and molecular docking methods. Studies revealed that TTH strongly quenches the intrinsic fluorophore of BSA by a static quenching mechanism. Time-resolved fluorescence spectra further confirmed the involvement of static quenching for TTH-BSA system. The calculated thermodynamic parameters; ΔH, ΔS, and ΔG showed that the binding process was spontaneous, exothermic and entropy driven. Synchronous fluorescence, three-dimensional (3D) fluorescence and circular dichroism data revealed that TTH induces the structural alteration in BSA and enhances its stability. In silico study of TTH-BSA system showed that it binds with BSA at the site I of subdomain IIA. Both the experimental and in silico study showed that the hydrophobic and electrostatic interactions play a major role in TTH-BSA binding.

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“…binding energy. (Kumari, Singh et al 2017;Vishvakarma, Patel et al 2017;Vishvakarma, Singh et al 2017;Kumar, Singh et al 2019;Vishvakarma, Shukla et al 2019;Vishvakarma, Singh et al 2019;Vishvakarma, Kumari et al 2020) This binding energy is due to contribution by the hydrogen bonding, van der Waal's and electrostatic interaction between the amino-acids of the receptor and the small molecules. (Hsu, Chen et al 2011) The visualization of the interaction was studied using Discovery Studio Visualizer.…”

Section: Molecular Dockingmentioning

confidence: 99%

Kuwanons, Promising inhibitors against the ACE-2, main protease of SARS-CoV-2 and falcipan-2 using molecular docking

Kumari

Kumar

et al. 2020

Preprint

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In the present scenario, the COVID-19 has affected the nations throughout the world. Till date, neither a vaccine nor a potential medicine is available for the cure from SARS-CoV-2 infection. Main protease of SARS-CoV-2 is responsible for the replication and transcription. Further, this virus binds to the angiotensin converting enzyme-2 (ACE-2) so there is need to find molecule, to avoid the binding of novel virus to ACE-2. It is reported that the molecules binds to falcipan-2 can help in the reduction of infection due to SARS-CoV-2. Therefore, there is a need to find promising candidate against the receptors, spread COVID-19. In the present work, kuwanons are proposed to be promising candidates against the main protease of SARS-CoV-2, ACE-2 and falcipan-2. The interaction between the different kuwanons with different receptors has been studied using the binding energy. Kuwanon M was found to best inhibitor against the main protease of SARS-CoV-2 and ACE-2. Further, the drug-likeness properties of all the 16 kuwanons were studied. Kuwanon-M found to be best inhibitor against the ACE-2 and main protease of SARS-CoV-2 with binding energy of -165.349 and -149.952 kcal/mol respectively while kuwanon-G found out to promising against the falcipan-2 with a binding energy of -149.573 kcal/mol.

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Effect of N‐Butyl‐N‐Methyl‐Morpholinium Bromide Ionic Liquid on the Conformation Stability of Human Serum Albumin

Cited by 56 publications

References 82 publications

Esterase activity and conformational changes of bovine serum albumin toward interaction with mephedrone: Spectroscopic and computational studies

Esterase activity and conformational changes of bovine serum albumin toward interaction with mephedrone: Spectroscopic and computational studies

Effect of triazole‐tryptophan hybrid on the conformation stability of bovine serum albumin

Kuwanons, Promising inhibitors against the ACE-2, main protease of SARS-CoV-2 and falcipan-2 using molecular docking

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