Saudi Journal of Biological Sciences (Feb 2024)

Alleviation of carbendazim toxicity effect by Moringa oleifera oil and Linum usitatissimum L. oil on testes of male rats: Physiological, histological and in silico study

  • Muhammad Hashim,
  • Atef M. Al-Attar,
  • Mohammed Y. Alomar,
  • Abdulkader M. Shaikh Omar,
  • Naser A. Alkenani,
  • Isam M. Abu Zeid

Journal volume & issue
Vol. 31, no. 2
p. 103921

Abstract

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Carbendazim (CBZ) is a widely used fungicide that is used to control the unwanted growth of fungi on fruits and vegetables. Sixty male rats were divided into six groups, each having ten. Group one served as control, animals belonging to group two were exposed to CBZ in the measure of 200 mg/kg body weight (BW). In the third and fourth groups, rats were administered 800 mg/kg BW of Moringa oleifera (moringa oil) and Linum usitatissimum L. (flaxseed oil), plus CBZ with the same dose given to group two. Groups five and six were administered with moringa and flaxseed oils respectively for six weeks. A marked decline was seen in oxidative stress markers, reduced glutathione (GSH), superoxide dismutase (SOD), catalase (CAT), and a rise in malondialdehyde (MDA) level in group two with severe histological disruptions. Moringa oil and flaxseed oil were used to alleviate these changes. In addition, a biocomputational molecular docking analysis of three proteins found in male rats was performed. In relation to CBZ (CID:10584007) the screened proteins namely testis-expressed protein (TX101_RAT), EPPI_RAT, and glutathione peroxidase 5 (GPX5_RAT) were docked, and their docking score were obtained (−5.9 kcal/mol), (−5.8 kcal/mol) and (−5.6 kcal/mol) respectively. By examining these interactions in 2D and 3D structures, a detailed understanding of the unique and specific binding affinity, hydrogen bonds, hydrophobic interactions, ionic bonds, and water bonds were obtained. Structure-based virtual screening (SBVS) molecular docking analysis showed that protein interaction with CBZ causes reproductive complications in protein expression and functions by hampering their normal function and blocking active sites.

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