A Non Glutathione Dependent Mechanism for Diphenyl Diselenide in Its Protection against Oxidative Assaults on Cerebral Lipids

Literatures have reported that the pharmacological mechanism of diphenyl diselenide (DPDS) is strictly dependent on its ability to mimic the endogenous antioxidant enzyme, glutathione peroxidase (GPx), utilizing reduced glutathione (GSH) to deactivate hydroperoxides. However, in the present study, we investigated the strict dependence of DPDS on GSH utilization via its GPx mimetic ability by monitoring the level oxidative damage in cerebral lipids subjected to oxidative assaults induced by Iron (II), Sodium nitroprusside (SNP), Hydrogen peroxide (H2O2) and Sodium oxalate. Results showed that DPDS markedly inhibited the peroxidation of cerebral lipids both in the presence and absence of GSH irrespective of the prooxidant employed for oxidative damage, suggesting that DPDS may utilize dual pharmacological mechanisms to combat oxidative assaults on biological macromolecules. We speculate that in vitro, DPDS preferentially utilize GPx mimic to prevent radical assaults on cerebral lipids when GSH is available. However, in the absence of GSH, DPDS possibly switch to a possible non-glutathione American Journal of Research Communication www.usa-journals.com Ogunmoyole, et al., 2015: Vol 3(9) 138 dependent mechanism to inhibit peroxidation of cerebral lipids. From the foregoing, we conclude that DPDS could switch between two mechanisms (GSH-dependent and non GSH dependent) both with similar but potent antioxidant efficacy.