Studies on conformational changes induced by binding of pendimethalin with human serum albumin

Potshangbam, Angamba Meetei; Javed, Mehjbeen; Ahmad, Masood

doi:10.1016/j.chemosphere.2019.125270

Cited by 39 publications

(10 citation statements)

References 49 publications

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“…For the purpose of determining the inhibition type of NDP for BLC, changes in BLC activity were monitored in the presence of three concentrations of NDP (0, 33.3, 66.7 μM). Different kinetic parameters were identified using the following given equations [ 37 ] :

v_{0} goodbreak= \frac{V_{\max} ([], S)}{K_{m} + ([], S)}

K_{cat} goodbreak= \frac{V_{italicmax}}{{([], E)}_{t}}

where the

v_{0}

and

V_{\max}

values represent the initial and final velocities, respectively. The K cat value is catalytic constant and the K m value is the Michaelis–Menten constant.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

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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v_{0} goodbreak= \frac{V_{\max} ([], S)}{K_{m} + ([], S)}

K_{cat} goodbreak= \frac{V_{italicmax}}{{([], E)}_{t}}

where the

v_{0}

and

V_{\max}

values represent the initial and final velocities, respectively. The K cat value is catalytic constant and the K m value is the Michaelis–Menten constant.…”

Section: Resultsmentioning

confidence: 99%

“…[11] For the purpose of determining the inhibition type of NDP for BLC, changes in BLC activity were monitored in the presence of three concentrations of NDP (0, 33.3, 66.7 μM). Different kinetic parameters were identified using the following given equations [37] :…”

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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show abstract

“…[67] Secondary structure is allied with the biological function of proteins. [68] Thus, to explore the effect of CuO NPs on the conformation changes of HSA, HHb, and Lys, the CD signals of these proteins were recorded without and with the addition of CuO NPs. HSA, HHb, and Lys give two characteristic negative CD spectra at 208 and 222 nm wavelengths, as shown in Figure 23.…”

Section: Binding Mode and Acting Forcesmentioning

confidence: 99%

“…Circular dichroism (CD) spectroscopy is one of the suitable techniques used in chemistry and biology to determine the secondary structure of the protein [67] . Secondary structure is allied with the biological function of proteins [68] . Thus, to explore the effect of CuO NPs on the conformation changes of HSA, HHb, and Lys, the CD signals of these proteins were recorded without and with the addition of CuO NPs.…”

Section: Interaction Of Cuo Nps With Hsa Hhb and Lysmentioning

confidence: 99%

Green Synthesis, in vitro Cytotoxicity, Antioxidant Activity and Interaction Studies of CuO Nanoparticles with DNA, Serum Albumin, Hemoglobin and Lysozyme

2022

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The present study reports an environmentally safe synthesis of CuO NPs employing Echinophora platyloba DC extract. The production of CuO NPs was authenticated using various analytical characterization techniques such as FT-IR, TEM, XRD, SEM-EDX, DLS, zeta potential, and UV-Vis. The DPPH assay was employed to assess the scavenging efficacy of synthesized CuO NPs. The results of the MTT assay exhibited that CuO NPs have efficient anticancer potential on two used cancer cell lines (MCF-7 and Burkitt's lymphoma). Thus, it tempts us to study the synthesized CuO NPs biocompatible aspects by interactions with several biologically significant molecules. The present experimental evidence demonstrates the direct interaction of CuO NPs with DNA, which might be one of the credible highways elevating its anticancer potential. Moreover, we investigated the interaction of CuO NPs with the most important blood proteins (HSA, HHb, and Lys) in simulated physiological conditions using spectroscopic methods. The interaction findings suggest that the native conformation of the above proteins was preserved at the level of secondary structure in spite of complex formations with CuO NPs. The binding constant values revealed the greater binding affinity of CuO NPs with HSA, HHb, and Lys as compared to ct-DNA; the binding affinity was found in the order HSA > HHb > Lys > ct-DNA.

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“…The UV-Vis technique is an excellent tool to verify the formation of a protein-ligand complex in the fundamental state and changes in the polypeptidic structure of the protein (Bratty, 2020;Santos et al, 2018). The formation of this complex is confirmed by changes in the characteristic wavelengths of the UV-Vis spectrum of the protein when it comes into contact with the test substance, such as changes in the absorption intensity and peak displacements (Ahmad et al, 2020;Đ ukić et al, 2020). Fig.…”

Section: Modulation Of the Hsa Uv-vis Spectra By Drmentioning

confidence: 99%

Probing the toxic interactions between the reactive dye Drimaren Red and Human Serum Albumin

Menezes

Assis

Neto

et al. 2021

Preprint

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Azo dyes like Drimaren Red CL-5B (DR, CI Reactive Red 241) represent a class of compounds extensively used in the textile industry and are extremely dangerous to the environment and human health. Therefore, understanding the binding characteristics between such substances and biological macromolecules is essential from a toxic-kinetic perspective. The molecular interaction between DR and Human Serum Albumin (HSA) was investigated through spectroscopic techniques and molecular docking approaches. The results indicate that DR quenches HSA fluorescence following a static mechanism (corroborated by UV-Vis studies) with a moderate interaction (Ka~105 M-1), guided by electrostatic interactions (DS> 0 and DH< 0). DR is 5.52 nm distant from fluorophore residue Trp-214 (according to FRET investigations), and the interaction is mainly related to Tyr residues (as revealed by synchronous fluorescence). The Ellman assay identified a decrease in the content of HSA free thiol. The results of the RLS demonstrate that there are HSA alterations, suggesting damage to the confirmation of the protein. Molecular docking suggests the binding site of DR was located in subdomain IIB HSA, corroborating the experimental properties. Finally, the results suggest a high potential for DR toxicity triggered by contact with key proteins, which affects the biomolecule functionalities.

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Studies on conformational changes induced by binding of pendimethalin with human serum albumin

Cited by 39 publications

References 49 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

Green Synthesis, in vitro Cytotoxicity, Antioxidant Activity and Interaction Studies of CuO Nanoparticles with DNA, Serum Albumin, Hemoglobin and Lysozyme

Probing the toxic interactions between the reactive dye Drimaren Red and Human Serum Albumin

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