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dc.creatorTrento, Marcus Vinícius Cardoso-
dc.creatorSales, Thais Aparecida-
dc.creatorAbreu, Tatiane Silva de-
dc.creatorBraga, Mariana Aparecida-
dc.creatorCesar, Pedro Henrique Souza-
dc.creatorMarques, Tamara Rezende-
dc.creatorMarcussi, Silvana-
dc.date.accessioned2020-05-18T16:08:24Z-
dc.date.available2020-05-18T16:08:24Z-
dc.date.issued2019-11-
dc.identifier.citationTRENTO, M. V. C. et al. Exploring the structural and functional aspects of the phospholipase A2 from Naja spp. International Journal of Biological Macromolecules, [S.l.], v. 140, p. 49-28, Nov. 2019.pt_BR
dc.identifier.urihttps://www.sciencedirect.com/science/article/pii/S0141813019335391pt_BR
dc.identifier.urihttp://repositorio.ufla.br/jspui/handle/1/41029-
dc.description.abstractNaja spp. venom is a natural source of active compounds with therapeutic application potential. Phospholipase A2 (PLA2) is abundant in the venom of Naja spp. and can perform neurotoxicity, cytotoxicity, cardiotoxicity, and hematological disorders. The PLA2s from Naja spp. venoms are Asp 49 isoenzymes with the exception of PLA2 Cys 49 from Naja sagittifera. When looking at the functional aspects, the neurotoxicity occurs by PLA2 called β-toxins that have affinity for phosphatidylcholine in nerve endings and synaptosomes membranes, and by α-toxins that block the nicotinic acetylcholine receptors in the neuromuscular junctions. In addition, these neurotoxins may inhibit K+ and Ca++ channels or even interfere with the Na+/K+/ATPase enzyme. The disturbance in the membrane fluidity also results in inhibition of the release of acetylcholine. The PLA2 can act as anticoagulants or procoagulant. The cytotoxicity exerted by PLA2s result from changes in the cardiomyocyte membranes, triggering cardiac failure and hemolysis. The antibacterial activity, however, is the result of alterations that decrease the stability of the lipid bilayer. Thus, the understanding of the structural and functional aspects of PLA2s can contribute to studies on the toxic and therapeutic mechanisms involved in the envenomation by Naja spp. and in the treatment of pathologies.pt_BR
dc.languageen_USpt_BR
dc.publisherElsevierpt_BR
dc.rightsrestrictAccesspt_BR
dc.sourceInternational Journal of Biological Macromoleculespt_BR
dc.subjectSnake venom toxinspt_BR
dc.subjectStructural domainspt_BR
dc.subjectActivity on membranespt_BR
dc.titleExploring the structural and functional aspects of the phospholipase A2 from Naja spppt_BR
dc.typeArtigopt_BR
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