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Garlic
Published in Robert E.C. Wildman, Richard S. Bruno, Handbook of Nutraceuticals and Functional Foods, 2019
Sharon A. Ross, Craig S. Charron
As proof of principle, in an in vitro setting, GSSA was found to react with the thiol-containing proteins papain and alcohol dehydrogenase from Thermoanaerobium brockii and inhibit their activity, whereas both proteins were reactivated using either reducing agent dithiothreitol or 2-mercaptoethanol. The concomitant release of allylmercaptan in these reactions indicated that the thioallyl moiety binds to inactivated proteins just as allicin has been shown to do. It is interesting to note that one enzyme that may be similarly affected by allicin breakdown products (i.e., DATS, SAC) is squalene monooxygenase.65 Such activity may explain the antifungal properties of allicin, as squalene monooxygenase is an important enzyme for the formation of the fungal cell wall.66
Butenafine
Published in M. Lindsay Grayson, Sara E. Cosgrove, Suzanne M. Crowe, M. Lindsay Grayson, William Hope, James S. McCarthy, John Mills, Johan W. Mouton, David L. Paterson, Kucers’ The Use of Antibiotics, 2017
Russell E. Lewis, Nicholas D. Beyda, Dimitrios P. Kontoyiannis
Similar to the allylamine antifungals, butenafine inhibits ergosterol biosynthesis in susceptible fungi, leading to altered fungal membrane sterol composition and inhibition of fungal cell growth (Ryder, 1992; Rubin et al., 2002). The target of butenafine activity is squalene monooxygenase (epoxidase). This catalyzes the conversion of squalene to 2,3-oxidosqualene, which serves as a rate-limiting step in the fungal ergosterol biosynthesis pathway (Ryder, 1992; Rubin et al., 2002). At higher concentrations (e.g. > 12.5 mg/l), butenafine has been shown to accumulate in and disrupt the fungal cell membrane, leading to intracellular release of inorganic orthophosphate, cation loss, and lethal damage to the fungal cell wall (Iwatani et al., 1993; Mingeot-Leclercq et al., 2001).
The mechanisms and therapeutic targets of ferroptosis in cancer
Published in Expert Opinion on Therapeutic Targets, 2021
Long Ye, Fengyan Jin, Shaji K. Kumar, Yun Dai
The cyst(e)ine/GSH/GPX4 system is not the only anti-ferroptosis pathway. Coenzyme Q10 (CoQ10) and squalene, both derived from mevalonate metabolism, also exhibit an anti-ferroptosis property (Figure 2B). In the presence of FSP1, CoQ10 is reduced to CoQ10H2, which in turn exerts an antioxidant effect directly by reducing toxic molecules derived from LPO or indirectly by recruiting α-TOH, a ROS scavenger [26,27]. Thus, inhibition of FSP1 by iFSP or miR-214 decreases CoQ10H2 and promotes ferroptosis. MDM2 or MDMX down-regulates the protein level of FSP1 and impairs the cellular defense against LPO[28]. Squalene accumulation due to inhibition of squalene monooxygenase activity also protects cells from ferroptosis, suggesting its anti-ferroptosis function. In contrast, cells with squalene deficiency due to the inhibition of squalene synthase (SQS) are more sensitive to ferroptosis[29]. Interestingly, the SQS agonist FIN56 is also able to induce ferroptosis, probably via depletion of CoQ10[30]. Statins, the inhibitors of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, reduce the synthesis of CoQ10 by blocking the mevalonate pathway, therefore triggering ferroptosis[30]. Recently, it has been reported that CoQ10 also exists in the mitochondrial membrane where it can be reduced into CoQ10H2 by dihydroorotate dehydrogenase (DHODH), an event coupled with a reaction catalyzing oxidizing dihydroorotate (DHO) into orotate (OA) (Figure 2B). Thus, DHODH prevents mitochondria from LPO, an effect independent of its known function in pyrimidine synthesis, thereby preventing ferroptosis[31].
Olive oil and clove oil-based nanoemulsion for topical delivery of terbinafine hydrochloride: in vitro and ex vivo evaluation
Published in Drug Delivery, 2022
Uzma Gul, Muhammad Imran Khan, Asadullah Madni, Muhammad Farhan Sohail, Mubashar Rehman, Akhtar Rasul, Leena Peltonen
Terbinafine hydrochloride (TF-HCl) belongs to allylamines family of antifungal drugs. It causes fungal cell death by hindering the ergosterol synthesis in the fungal cells (Trichophyton mentagrophytes and Trichophyton rubrum). This is due to the inhibition of squalene monooxygenase enzyme activity, which prohibits the growth of fungus (Barot et al., 2012).