Abstract
Background: Proteins are the critical bio-molecules for cellular function and are also considered to be highly susceptible to reactive oxygen species (ROS)-induced oxidative damages.
Methods: The present study aimed to evaluate some simple water-soluble aliphatic organoselenium compounds bearing different functional groups but of similar carbon chain (propyl) length for a protective effect against 2,2’-azobis-(2-amidinopropane) dihydrochloride (AAPH)-induced oxidative damage using mitochondria as an in vitro model.
Results: The results indicated that APPH (20 mM) treatment of mitochondrial fraction induced protein carbonylation, leading to inactivation of redox enzymes and electron transport chain (ETC) and, ultimately the mitochondrial dysfunction. On the other hand, treatment with 0.5 mM of monoselenobutyric acid (SeBA) and monoselenopropyl alcohol (SePOH) significantly prevented APPH-induced protein carbonylation in mitochondrial fraction and restored activities of mitochondrial proteins. On the contrary, monoselenopropyl amine (SePAm) treatment at identical concentrations did not show significant protection to mitochondrial activity from AAPH-induced oxidative damages. The above results concur with the reported peroxyl radical scavenging activities of the above molecules.
Conclusion: In conclusion, SeBA and SePOH are potential candidate molecules to protect proteins from oxidative damage and, therefore, can be useful for managing oxidative stress in cellular models.
Keywords: Organoselenium, AAPH, reactive oxygen species, mitochondrial proteins, oxidative damage, SeBA, SePOH.
Graphical Abstract
[http://dx.doi.org/10.1038/nature12985] [PMID: 24429632]
[http://dx.doi.org/10.1155/2012/329635]
[http://dx.doi.org/10.1155/2018/7857251] [PMID: 30057684]
[http://dx.doi.org/10.1007/s11356-013-1748-0] [PMID: 23636598]
[http://dx.doi.org/10.1016/j.molcel.2016.02.011] [PMID: 26942671]
[PMID: 25206509]
[http://dx.doi.org/10.1080/10715762.2021.1882678] [PMID: 33555213]
[http://dx.doi.org/10.1246/cl.200015]
[http://dx.doi.org/10.3109/10715762.2010.543678] [PMID: 21235282]
[http://dx.doi.org/10.1021/tx700137a] [PMID: 17900173]
[http://dx.doi.org/10.1016/j.freeradbiomed.2006.09.002] [PMID: 17145558]
[http://dx.doi.org/10.1016/j.febslet.2004.10.061]
[http://dx.doi.org/10.1016/j.freeradbiomed.2021.08.017] [PMID: 34425189]
[http://dx.doi.org/10.1006/abbi.1993.1311] [PMID: 8390225]
[http://dx.doi.org/10.1186/s12937-016-0186-5] [PMID: 27456681]
[http://dx.doi.org/10.1039/C5OB01665G] [PMID: 26372527]