Use este identificador para citar ou linkar para este item: http://www.alice.cnptia.embrapa.br/alice/handle/doc/1150743
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dc.contributor.authorFRIHLING, B. E. F.
dc.contributor.authorBOLETI, A. P. de A.
dc.contributor.authorOLIVEIRA, C. F. R. de
dc.contributor.authorSANCHES, S. C.
dc.contributor.authorCARDOSO, P. H. de O.
dc.contributor.authorVERBISCK, N. V.
dc.contributor.authorMACEDO, M. L. R.
dc.contributor.authorSANTA RITA, P. H.
dc.contributor.authorCARVALHO, C. M. E.
dc.contributor.authorMIGLIOLO, L.
dc.date.accessioned2023-01-06T18:01:18Z-
dc.date.available2023-01-06T18:01:18Z-
dc.date.created2023-01-06
dc.date.issued2022
dc.identifier.citationPharmaceuticals, v. 15, n. 6, article 724, 2022.
dc.identifier.urihttp://www.alice.cnptia.embrapa.br/alice/handle/doc/1150743-
dc.descriptionNature presents a wide range of biomolecules with pharmacological potential, including venomous animal proteins. Among the protein components from snake venoms, phospholipases (PLA2) are of great importance for the development of new anticancer compounds. Thus, we aimed to evaluate the PLA2 anticancer properties from Bothrops moojeni venom. The crude venom was purified through three chromatographic steps, monitored by enzymatic activity and SDS-PAGE (12%). The purified PLA2 denominated BmPLA2 had its molecular mass and N-terminal sequence identified by mass spectrometry and Edman degradation, respectively. BmPLA2 was assayed against human epithelial colorectal adenocarcinoma cells (Caco-2), human rhabdomyosarcoma cells (RD) and mucoepidermoid carcinoma of the lung (NCI-H292), using human fibroblast cells (MRC-5) and microglia cells (BV-2) as a cytotoxicity control. BmPLA2 presented 13,836 Da and a 24 amino acid-residue homologue with snake PLA2, which showed a 90% similarity with other Bothrops moojeni PLA2. BmPLA2 displayed an IC50 of 0.6 M against Caco-2, and demonstrated a selectivity index of 1.85 (compared to MRC-5) and 6.33 (compared to BV-2), supporting its selectivity for cancer cells. In conclusion, we describe a new acidic phospholipase, which showed antitumor activity and is a potential candidate in the development of new biotechnological tools.
dc.language.isoeng
dc.rightsopenAccess
dc.titlePurification, characterization and evaluation of the antitumoral activity of a phospholipase A2 from the snake Bothrops moojeni.
dc.typeArtigo de periódico
dc.subject.thesagroBiotecnologia
dc.subject.thesagroEspectrometria
dc.subject.thesagroProteína
dc.subject.nalthesaurusAnimal proteins
dc.subject.nalthesaurusBiotechnology
dc.subject.nalthesaurusBothrops
dc.subject.nalthesaurusCell membranes
dc.subject.nalthesaurusMass spectrometry
dc.subject.nalthesaurusPhospholipase A2
dc.description.notesNa publicação: Newton Verbisck.
riaa.ainfo.id1150743
riaa.ainfo.lastupdate2023-01-06
dc.identifier.doihttps://doi.org/10.3390/ph15060724
dc.contributor.institutionBRENO EMANUEL FARIAS FRIHLING, UNIVERSIDADE CATÓLICA DOM BOSCO; ANA PAULA DE ARAÚJO BOLETI, UNIVERSIDADE CATÓLICA DOM BOSCO; CAIO FERNANDO RAMALHO DE OLIVEIRA, UNIVERSIDADE FEDERAL DE MATO GROSSO DO SUL; SIMONE CAMARGO SANCHES, UNIVERSIDADE CATÓLICA DOM BOSCO; PEDRO HENRIQUE DE OLIVEIRA CARDOSO, UNIVERSIDADE CATÓLICA DOM BOSCO; NEWTON VALERIO VERBISCK, CNPGC; MARIA LÍGIA RODRIGUES MACEDO, UNIVERSIDADE FEDERAL DE MATO GROSSO DO SUL; PAULA HELENA SANTA RITA, UNIVERSIDADE CATÓLICA DOM BOSCO; CRISTIANO MARCELO ESPINOLA CARVALHO, UNIVERSIDADE CATÓLICA DOM BOSCO; LUDOVICO MIGLIOLO, UNIVERSIDADE FEDERAL DO RIO GRANDE DO NORTE.
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