Molecular Assessment of the Toxic Mechanism of the Latest Neonicotinoid Dinotefuran with Glutathione Peroxidase 6 from Arabidopsis thaliana

Abstract

With widespread applications of the latest neonicotinoid in agriculture, dinotefuran has gradually become a hazardous contaminant for plants through the generation of excessive reactive oxygen species. However, the potential toxic mechanisms of oxidative damages to plants induced by dinotefuran are still unknown. As a core component of the glutathione antioxidant enzyme system, glutathione peroxidases have been used as biomarkers to reflect excessive oxidative stress. In this study, the hazardous effects of dinotefuran on AtGPX6 were investigated at the molecular level. The intrinsic fluorescence intensity of AtGPX6 was quenched using the static quenching mechanism upon binding with dinotefuran. Moreover, a single binding site was predicted for AtGPX6 toward dinotefuran, and the complex formation was presumed to be driven by hydrogen bonds or van der Waals forces, which conformed with the molecular docking results. In addition, AtGPX6 exhibited moderate binding affinity with dinotefuran based on the bio-layer interferometry assay. In addition, the loosening and unfolding of the protein skeleton of AtGPX6 with the addition of dinotefuran were explored along with the increase of hydrophobicity around tryptophan residues. Lastly, the toxic effects of dinotefuran on the root growth of Arabidopsis seedlings were also examined. The exploration of the binding mechanism of dinotefuran with AtGPX6 at the molecular level would provide the toxicity assessment of dinotefuran on plants.

Evaluation of the Two Typical Diamide Insecticide-Induced Oxidative Damages and the Molecular Mechanism Underlying Their Toxicity in Triticum aestivum

“…Moreover, flubendiamide exhibited significantly stronger binding affinity ( K D ) with Ta GSTF1 than chlorantraniliprole, so it was inferred that flubendiamide imposed more powerful impacts on Ta GSTF1 than chlorantraniliprole. In addition, Ta GSTF1 displayed much higher affinity constants for both flubendiamide and chlorantraniliprole in comparison with the reported affinity constant ( K D ) of 900 μM between the other glutathione S -transferase At GSTF8 and nicotinic insecticide dinotefuran …”

“…In addition, TaGSTF1 displayed much higher affinity constants for both flubendiamide and chlorantraniliprole in comparison with the reported affinity constant (K D ) of 900 μM between the other glutathione S-transferase AtGSTF8 and nicotinic insecticide dinotefuran. 36 Conformational Investigations on TaGSTF1. The correct corresponding structure of the protein is dominant for the accurate performance of the specific biological function.…”

“…Glutathione S -transferases (GSTs) have displayed indispensable functions on protection from oxidative impairments. , However, GSTs are not limited to peroxide scavenging, and they can also combine reduced glutathione with electrophilic groups to detoxify a wide variety of toxic substances including insecticides. To explore toxic impacts of flubendiamide and chlorantraniliprole on protein functions accompanied with structural alterations, the activity changes of Ta GSTF1 after dealing with flubendiamide and chlorantraniliprole were determined separately.…”

Dendrochronology reveals different effects among host tree species from feeding by Lycorma delicatula (White)

“…However, there has been no evidence reported for elevated plant function by dinotefuran. In fact, this insecticide has been shown to have a negative effect on plant roots ( 44 ) and increases oxidative stress in plants ( 45 ). It is unlikely, then, that the dinotefuran application itself was responsible for the larger tree ring growth noted in dinotefuran-treated trees.…”

The Automatic Sampler for UV Spectroscopy Toxicity Detection: Based on the Perspective of Binding Information with the Carrier Protein

“…temperature has a greater limitation on the experimental results, which is the main cause of protein denaturation. In the design of fluorescence experiments, we often control the temperature of the drug's toxicity to human serum albumin within 37°C [4], and the temperature of the drug's toxicity to glutathione peroxidase is best controlled within 27°C [5]. Otherwise, it is difficult to determine what is the dominant factor leading to changes in the carrier protein structure.…”