Study on the binding mechanism of thiamethoxam with three model proteins:spectroscopic studies and theoretical simulations

Su, Xiao Dong; Wang, Leng; Xu, Yefei; Dong, Lili; Lu, Huizhe

doi:10.1016/j.ecoenv.2020.111280

Cited by 10 publications

(7 citation statements)

References 34 publications

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“…We further explored the binding site of trans- resveratrol on HSA using site markers, warfarin, and ibuprofen. These two site markers are routinely used probe molecules to locate the binding site of a small molecule on protein 35 . Most of the ligand binds to the protein at Sudlow’s site I (subdomain IIA) and Sudlow’s site 2 (subdomain IIIA).…”

Section: Resultsmentioning

confidence: 99%

Investigating binding dynamics of trans resveratrol to HSA for an efficient displacement of aflatoxin B1 using spectroscopy and molecular simulation

Qureshi

Javed

2022

Sci Rep

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Resveratrol is a polyphenol belonging to the class stilbenes. The active and stable form of resveratrol is trans-resveratrol. This polyphenol is bestowed with numerous biological properties. Aflatoxin B1 is a hepato-carcinogen and mutagen that is produced by Aspergillus species. In this study, the interaction of trans-resveratrol with HSA followed by competitive dislodging of AFB1 from HSA by trans-resveratrol has been investigated using spectroscopic studies. The UV-absorption studies revealed ground state complex formation between HSA and trans-resveratrol. Trans-resveratrol binds strongly to HSA with the binding constant of ~ 107 M−1 to a single binding site (n = 1.58), at 298.15 K. The Stern–Volmer quenching constant was calculated as 7.83 × 104 M−1 at 298.15 K, suggesting strong fluorescence quenching ability of trans-resveratrol. Site markers displacement assay projected subdomain IIA as the binding site of trans-resveratrol to HSA. The molecular docking approach envisages the amino acid residues involved in the formation of the binding pocket. As confirmed from the site marker displacement assays, both trans-resveratrol and AFB1 binds to HSA in the same binding site, subdomain IIA. The study explores the ability of trans-resveratrol to displace AFB1 from the HSA-AFB1 complex, thereby affecting the toxicokinetic behavior of AFB1 associated with AFB1 exposure.

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Section: Resultsmentioning

confidence: 99%

Investigating binding dynamics of trans resveratrol to HSA for an efficient displacement of aflatoxin B1 using spectroscopy and molecular simulation

Qureshi

Javed

2022

Sci Rep

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“…44,45 Warfarin and ibuprofen were used as site marker probes to investigate the binding site of AFB 1 on BSA with the help of fluorescence spectroscopy. 46 Warfarin and ibuprofen are welldistinguished site marker probes for BSA that bind to site I (subdomain IIA) and site II (subdomain IIIA) of BSA. BSA (5 μM) and AFB 1 (14 μM) were titrated with increasing site marker concentration.…”

Section: Resultsmentioning

confidence: 99%

“…Most of the xenobiotics are known to bind site I and site II since their interactions with these loci are of utmost sensitivity to the proton-induced neutral base transition of albumins. , Warfarin and ibuprofen were used as site marker probes to investigate the binding site of AFB 1 on BSA with the help of fluorescence spectroscopy . Warfarin and ibuprofen are well-distinguished site marker probes for BSA that bind to site I (subdomain IIA) and site II (subdomain IIIA) of BSA.…”

Section: Resultsmentioning

confidence: 99%

Aflatoxin B₁ Induced Structural and Conformational Changes in Bovine Serum Albumin: A Multispectroscopic and Circular Dichroism-Based Study

Qureshi

Javed

2021

ACS Omega

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Aflatoxin B 1 (AFB 1 ) is a mutagen that has been categorized as a group 1 human carcinogen by the International Agency for Research on Cancer. It is produced as a secondary metabolite by soil fungi Aspergillus flavus and Aspergillus parasiticus. Here, in this study, the effect of AFB 1 on the structure and conformation of bovine serum albumin (BSA) using multispectroscopic tools like fluorescence spectroscopy, ultraviolet−visible absorption spectroscopy, and circular dichroism spectropolarimetry has been ascertained. Ultraviolet absorption spectroscopy revealed hyperchromicity in the absorption spectra of BSA in the presence of AFB 1 . The binding constant was calculated in the range of 10 4 M −1 , by fluorescence spectroscopy suggesting moderate binding of the toxin to BSA. The study also confirms the static nature of fluorescence quenching. The stoichiometry of binding sites was found to be unity. The competing capability of warfarin for AFB 1 was higher than ibuprofen as calculated from site marker displacement assay. Forster resonance energy transfer confirmed the high efficiency of energy transfer from BSA to AFB 1 . Circular dichroism spectropolarimetry showed a decrease in the α-helix in BSA in the presence of AFB 1 . The melting temperature of BSA underwent an increment in the presence of a mycotoxin from 62.5 to 70.3 °C. Molecular docking confirmed the binding of AFB 1 to subdomain IIA in BSA. ■ HIGHLIGHTS• In this study, binding dynamics of AFB 1 with BSA were explored by UV absorption spectroscopy, fluorescence spectroscopy, and molecular docking.• Molecular docking analysis substantiated that Arg-217, Tyr-149, Arg-256, and Ala-260 residues stabilize the interacting complex via hydrogen bonding.

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“…The unbiased molecular dynamics (MD) simulations carried out to understand the model structural of ONs bound to the small molecules. The experiment performed between two molecules (at 20 Å apart from each other) without any artificial force and placed in center of a truncated octahedral water box and 150 mM NaCl with a size of 64 × 64 × 64 Å 3 and balanced the counter charge sodium ions use in the complexes MD simulations through AMBER ff99bsc-OL15 force field [ 14 , 15 ] and general AMBER force field (GAFF) [ 11 , 16 ] with Amber16 code [ 17 , 18 ] scheduled in-time GPU clusters. On the other hand Åqvist potential [ 19 ] and TIP3P model [ 20 ] for the ions and water molecules, respectively.…”

Section: Methodsmentioning

confidence: 99%

Oligonucleotide nanoassemblies with allyl bromide scaffold-based small molecules

et al. 2023

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The development of oligonucleotide nanoassemblies with small molecules has shown great potential in bio-medical applications. However, the interaction of negatively charged oligonucleotides with halogenated small molecules represents a scientific challenge. Here, we introduced a distinct allyl bromide halogenated scaffold, which exhibits specific interaction with adenine nucleic bases of the oligonucleotides, thus leading to the formation of self-assembled nanostructures. Graphical abstract

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Study on the binding mechanism of thiamethoxam with three model proteins:spectroscopic studies and theoretical simulations

Cited by 10 publications

References 34 publications

Investigating binding dynamics of trans resveratrol to HSA for an efficient displacement of aflatoxin B1 using spectroscopy and molecular simulation

Investigating binding dynamics of trans resveratrol to HSA for an efficient displacement of aflatoxin B1 using spectroscopy and molecular simulation

Aflatoxin B₁ Induced Structural and Conformational Changes in Bovine Serum Albumin: A Multispectroscopic and Circular Dichroism-Based Study

Oligonucleotide nanoassemblies with allyl bromide scaffold-based small molecules

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Study on the binding mechanism of thiamethoxam with three model proteins:spectroscopic studies and theoretical simulations

Cited by 10 publications

References 34 publications

Investigating binding dynamics of trans resveratrol to HSA for an efficient displacement of aflatoxin B1 using spectroscopy and molecular simulation

Investigating binding dynamics of trans resveratrol to HSA for an efficient displacement of aflatoxin B1 using spectroscopy and molecular simulation

Aflatoxin B1 Induced Structural and Conformational Changes in Bovine Serum Albumin: A Multispectroscopic and Circular Dichroism-Based Study

Oligonucleotide nanoassemblies with allyl bromide scaffold-based small molecules

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Product

Resources

About

Aflatoxin B₁ Induced Structural and Conformational Changes in Bovine Serum Albumin: A Multispectroscopic and Circular Dichroism-Based Study