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dc.creatorCosta, Tássia R.-
dc.creatorFrancisco, Aleff F.-
dc.creatorCardoso, Fábio F.-
dc.creatorMoreira-Dill, Leandro S.-
dc.creatorFernandes, Carlos A. H.-
dc.creatorGomes, Antoniel A. S.-
dc.creatorGuimarães, César L. S.-
dc.creatorMarcussi, Silvana-
dc.creatorPereira, Paulo S.-
dc.creatorOliveira, Hamine C.-
dc.creatorFontes, Marcos R. M.-
dc.creatorSilva, Saulo L.-
dc.creatorZuliani, Juliana P.-
dc.creatorSoares, Andreimar M.-
dc.date.accessioned2022-01-07T15:35:02Z-
dc.date.available2022-01-07T15:35:02Z-
dc.date.issued2021-08-31-
dc.identifier.citationCOSTA, T. R. et al. Gallic acid anti-myotoxic activity and mechanism of action, a snake venom phospholipase A2 toxin inhibitor, isolated from the medicinal plant Anacardium humile. International Journal of Biological Macromolecules, [S.l.], v. 185, p. 494-512, Aug. 2021. DOI: 10.1016/j.ijbiomac.2021.06.163.pt_BR
dc.identifier.urihttps://www.sciencedirect.com/science/article/pii/S0141813021013921pt_BR
dc.identifier.urihttp://repositorio.ufla.br/jspui/handle/1/48808-
dc.description.abstractSnakebite envenoming is the cause of an ongoing health crisis in several regions of the world, particularly in tropical and neotropical countries. This scenario creates an urgent necessity for new practical solutions to address the limitations of current therapies. The current study investigated the isolation, phytochemical characterization, and myotoxicity inhibition mechanism of gallic acid (GA), a myotoxin inhibitor obtained from Anacardium humile. The identification and isolation of GA was achieved by employing analytical chromatographic separation, which exhibited a compound with retention time and nuclear magnetic resonance spectra compatible with GA's commercial standard and data from the literature. GA alone was able to inhibit the myotoxic activity induced by the crude venom of Bothrops jararacussu and its two main myotoxins, BthTX-I and BthTX-II. Circular dichroism (CD), fluorescence spectroscopy (FS), dynamic light scattering (DLS), and interaction studies by molecular docking suggested that GA forms a complex with BthTX-I and II. Surface plasmon resonance (SPR) kinetics assays showed that GA has a high affinity for BthTX-I with a KD of 9.146 × 10−7 M. Taken together, the two-state reaction mode of GA binding to BthTX-I, and CD, FS and DLS assays, suggest that GA is able to induce oligomerization and secondary structure changes for BthTX-I and -II. GA and other tannins have been shown to be effective inhibitors of snake venoms' toxic effects, and herein we demonstrated GA's ability to bind to and inhibit a snake venom PLA2, thus proposing a new mechanism of PLA2 inhibition, and presenting more evidence of GA's potential as an antivenom compound.pt_BR
dc.languageen_USpt_BR
dc.publisherElsevierpt_BR
dc.rightsrestrictAccesspt_BR
dc.sourceInternational Journal of Biological Macromoleculespt_BR
dc.subjectGallic acidpt_BR
dc.subjectSnake venomspt_BR
dc.subjectPhospholipase A2 inhibitorpt_BR
dc.titleGallic acid anti-myotoxic activity and mechanism of action, a snake venom phospholipase A2 toxin inhibitor, isolated from the medicinal plant Anacardium humilept_BR
dc.typeArtigopt_BR
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