A spectroscopic and molecular dynamics simulation approach towards the stabilizing effect of ammonium-based ionic liquids on bovine serum albumin

Satish, Lakkoji; Millan, Sabera; Bera, Krishnendu; Mohapatra, Sujata; Sahoo, Harekrushna

doi:10.1039/c7nj02900d

Cited by 46 publications

(12 citation statements)

References 73 publications

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“…The intrinsic fluctuations present in the BSA backbone in the aqueous system are in agreement with the previous study. 52 Domain I and III of BSA are more flexible in comparison to domain II. The addition of reline in water induces enhanced fluctuations at both the studied concentrations.…”

Section: Resultsmentioning

confidence: 99%

Structural adaptations in the bovine serum albumin protein in archetypal deep eutectic solvent reline and its aqueous mixtures

Kumari

Kashyap

2022

Phys. Chem. Chem. Phys.

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Section: Resultsmentioning

confidence: 99%

Structural adaptations in the bovine serum albumin protein in archetypal deep eutectic solvent reline and its aqueous mixtures

Kumari

Kashyap

2022

Phys. Chem. Chem. Phys.

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“…The Tyr‐411, Lys‐413, and Lys‐414 amino acid residues of BSA are located in site II (subdomain IIIA), have catalytic cleavage mechanisms, and contribute in esterase‐like activity of BSA. Tyr‐411 is the first amino acid residue of BSA which rapidly acetylated by PNPA . In this respect, the binding sites of drugs with the substrate (PNPA) are closely related to inhibition of drugs on major esterase‐like activities of BSA.…”

Section: Resultsmentioning

confidence: 99%

“…Molecular docking is a modern analysis tool for scientific research to validate the ligand and protein interaction; hence, molecular docking has been performed to study the precise binding modes of 4MMC on BSA by using the AutoDock 4.2 . The probable conformations of the 4MMC and BSA complex were considered by using AutoDock program.…”

Section: Resultsmentioning

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 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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“…In addition to experimental approaches for evaluating the effect on ILs on the protein stability, various in silico analyses have also been performed. For instance, a study using molecular dynamics simulation analysis indicated that in the presence of ILs the bovine serum albumin does not destabilize the structure it adopts, which was also confirmed by experimental analysis [ 206 ]. These molecular dynamics simulations will undoubtedly help to narrow the field of potential IL candidates for specific protein and biomolecular applications.…”

Section: Conclusion/perspectivementioning

confidence: 81%

Effects of Ionic Liquids on Metalloproteins

et al. 2021

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In the past decade, innovative protein therapies and bio-similar industries have grown rapidly. Additionally, ionic liquids (ILs) have been an area of great interest and rapid development in industrial processes over a similar timeline. Therefore, there is a pressing need to understand the structure and function of proteins in novel environments with ILs. Understanding the short-term and long-term stability of protein molecules in IL formulations will be key to using ILs for protein technologies. Similarly, ILs have been investigated as part of therapeutic delivery systems and implicated in numerous studies in which ILs impact the activity and/or stability of protein molecules. Notably, many of the proteins used in industrial applications are involved in redox chemistry, and thus often contain metal ions or metal-associated cofactors. In this review article, we focus on the current understanding of protein structure-function relationship in the presence of ILs, specifically focusing on the effect of ILs on metal containing proteins.

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A spectroscopic and molecular dynamics simulation approach towards the stabilizing effect of ammonium-based ionic liquids on bovine serum albumin

Abstract: Experimental and theoretical evidence in support of the stabilizing effect of ammonium-based ionic liquids on thermal unfolding/refolding of bovine serum albumin is provided in this article.

Cited by 46 publications

References 73 publications

Structural adaptations in the bovine serum albumin protein in archetypal deep eutectic solvent reline and its aqueous mixtures

Structural adaptations in the bovine serum albumin protein in archetypal deep eutectic solvent reline and its aqueous mixtures

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

Effects of Ionic Liquids on Metalloproteins

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