Solvent-dependent binding interactions of the organophosphate pesticide, chlorpyrifos (CPF), and its metabolite, 3,5,6-trichloro-2-pyridinol (TCPy), with Bovine Serum Albumin (BSA): A comparative fluorescence quenching analysis

Dahiya, Vandana; Chaubey, Bhawna; Dhaharwal, Ashok K.; Pal, Samanwita

doi:10.1016/j.pestbp.2017.04.011

Cited by 28 publications

(9 citation statements)

References 43 publications

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“…Literature reports support that a shift in the emission spectrum to shorter wavelengths with a progressive increase in quencher concentrations is mainly attributed to the fluorescence quenching of Trp residues buried deep inside the protein’s hydrophobic core. 29 , 30 Also, it is interesting to note that the fluorescence intensities of BSA and HSA decreased to approximately 19.15 and 29.93%, respectively, with the addition of Cu(II) at pH 7.4.…”

Section: Resultsmentioning

confidence: 99%

Probing the Role of Cu(II) Ions on Protein Aggregation Using Two Model Proteins

John

Mathew²,

Mathew

et al. 2021

ACS Omega

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Copper is an essential trace element for human biology where its metal dyshomeostasis accounts for an increased level of serum copper, which accelerates protein aggregation. Protein aggregation is a notable feature for many neurodegenerative disorders. Herein, we report an experimental study using two model proteins, bovine serum albumin (BSA) and human serum albumin (HSA), to elucidate the mechanistic pathway by which serum albumins get converted from a fully folded globular protein to a fibril and an amorphous aggregate upon interaction with copper. Steady-state fluorescence, time-resolved fluorescence studies, and Raman spectroscopy were used to monitor the unfolding of serum albumin with increasing copper concentrations. Steady-state fluorescence studies have revealed that the fluorescence quenching of BSA/HSA by Cu(II) has occurred through a static quenching mechanism, and we have evaluated both the quenching constants individually. The binding constants of BSA–Cu(II) and HSA–Cu(II) were found to be 2.42 × 10 4 and 0.05 × 10 4 M –1 , respectively. Further nanoscale morphological changes of BSA mediated by oligomers to fibril and HSA to amorphous aggregate formation were studied using atomic force microscopy. This aggregation process correlates with the Stern–Volmer plots in the absence of discernible lag phase. Raman spectroscopy results obtained are in good agreement with the increase in antiparallel β-sheet structures formed during the aggregation of BSA in the presence of Cu(II) ions. However, an increase in α-helical fractions is observed for the amorphous aggregate formed from HSA.

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Section: Resultsmentioning

confidence: 99%

Probing the Role of Cu(II) Ions on Protein Aggregation Using Two Model Proteins

John

Mathew²,

Mathew

et al. 2021

ACS Omega

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“…The binding mechanism of the drug ligand interaction to SA in terms of its dissociation constant and the half-life of the ligand–protein complex has always been of great interest in pharmaceutical industries as these parameters affect the delivery of the molecule to the target tissues. If the binding is too strong, the availability of that ligand in plasma will be reduced and hence lead to slower diffusion of the ligand to the target . Because of their slow distribution, a high dose of these drugs will be required in vivo for their efficient mode of action at target tissues .…”

Section: Discussionmentioning

confidence: 99%

“…However, DFBA being a molecular fragment exhibits excellent water solubility, allowing protein interaction analysis to be carried out in aqueous media. Additionally, DFBA may exert an adverse effect on binding to various biologically active proteins, being a metabolite of several pesticides …”

Section: Introductionmentioning

confidence: 99%

“…Additionally, DFBA may exert an adverse effect on binding to various biologically active proteins, being a metabolite of several pesticides. 36 A well-characterized binding mechanism with a soluble fragment would therefore allow understanding of the effect of the pesticide or it may also help in developing lead molecules from these fragments that can be a target-specific hit for challenging receptors. 37,38 Therefore, it becomes an interesting choice to monitor the interaction of DFBA with serum proteins.…”

Section: Introductionmentioning

confidence: 99%

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Binding Interaction of Organofluorine–Serum Albumin: A Comparative Ligand-Detected ¹⁹F NMR Analysis

Chaubey

Pal

2018

J. Phys. Chem. B

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In the present study, we attempt to characterize fluorinated ligand-serum albumin interaction in solution by a set of one-dimensional F ligand-based experiments. In this regard, a model system diflunisal (DFL)-human serum albumin (HSA) has been chosen to benchmark the utility ofF relaxation and diffusion-based experiments in deciphering ligand-protein interactions. Further, we extend the application of a similar set of F experiments to unravel the molecular interaction in an unexplored system of 2,6-difluorobenzoic acid (DFBA)-bovine serum albumin (BSA). Interaction analysis of DFBA-SA is of particular interest because DFBA is not only a stable metabolite of a number of pesticides but also used as the starting reagent of many fluorinated drugs. Observation ofF-H & H-H saturation transfer difference effects confirmed binding of the ligands to SA. Further, these ligand-protein complexes were probed in terms of the dissociation constant ( K), number of binding sites ( n), bound fraction of the ligand ( P), the complex lifetime (τ), and exchange rate ( K). Although Carr-Purcell-Meiboom-Gill (CPMG)-based transverse relaxation and diffusion analysis quantified the former three quantities, the latter two were determined by the constant time fast pulsing CPMG method. Additionally, F competition binding experiments performed with well-characterized BSA site markers and DFBA indicated nonspecific binding of DFBA to BSA, whereas similar measurements in the case of HSA with DFL and DFBA revealed superior binding interaction of DFL with SA.

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“…For static quenching, K SV is the association constant of the quencher-uorophore ground-state complex. 31,32 Plots of F 0 /F against 1/[Q] of TGB quencher with HSA and BSA are shown in Fig. S3.…”

Section: Characterization Of the Tgb-hsa And Tgb-bsa Bindingmentioning

confidence: 99%

Insights into the interaction mechanism between tiagabine hydrochloride and two serum albumins

2018

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Solvent-dependent binding interactions of the organophosphate pesticide, chlorpyrifos (CPF), and its metabolite, 3,5,6-trichloro-2-pyridinol (TCPy), with Bovine Serum Albumin (BSA): A comparative fluorescence quenching analysis

Cited by 28 publications

References 43 publications

Probing the Role of Cu(II) Ions on Protein Aggregation Using Two Model Proteins

Probing the Role of Cu(II) Ions on Protein Aggregation Using Two Model Proteins

Binding Interaction of Organofluorine–Serum Albumin: A Comparative Ligand-Detected ¹⁹F NMR Analysis

Insights into the interaction mechanism between tiagabine hydrochloride and two serum albumins

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Solvent-dependent binding interactions of the organophosphate pesticide, chlorpyrifos (CPF), and its metabolite, 3,5,6-trichloro-2-pyridinol (TCPy), with Bovine Serum Albumin (BSA): A comparative fluorescence quenching analysis

Cited by 28 publications

References 43 publications

Probing the Role of Cu(II) Ions on Protein Aggregation Using Two Model Proteins

Probing the Role of Cu(II) Ions on Protein Aggregation Using Two Model Proteins

Binding Interaction of Organofluorine–Serum Albumin: A Comparative Ligand-Detected 19F NMR Analysis

Insights into the interaction mechanism between tiagabine hydrochloride and two serum albumins

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Binding Interaction of Organofluorine–Serum Albumin: A Comparative Ligand-Detected ¹⁹F NMR Analysis