Purification, characterization and evaluation of the antitumoral activity of a phospholipase A2 from the snake Bothrops moojeni.

Detalhes bibliográficos
Autor(a) principal: FRIHLING, B. E. F.
Data de Publicação: 2022
Outros Autores: BOLETI, A. P. de A., OLIVEIRA, C. F. R. de, SANCHES, S. C., CARDOSO, P. H. de O., VERBISCK, N. V., MACEDO, M. L. R., SANTA RITA, P. H., CARVALHO, C. M. E., MIGLIOLO, L.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)
Texto Completo: http://www.alice.cnptia.embrapa.br/alice/handle/doc/1150743
https://doi.org/10.3390/ph15060724
Resumo: Nature 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.
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spelling Purification, characterization and evaluation of the antitumoral activity of a phospholipase A2 from the snake Bothrops moojeni.BiotecnologiaEspectrometriaProteínaAnimal proteinsBiotechnologyBothropsCell membranesMass spectrometryPhospholipase A2Nature 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.Na publicação: Newton Verbisck.BRENO 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.FRIHLING, B. E. F.BOLETI, A. P. de A.OLIVEIRA, C. F. R. deSANCHES, S. C.CARDOSO, P. H. de O.VERBISCK, N. V.MACEDO, M. L. R.SANTA RITA, P. H.CARVALHO, C. M. E.MIGLIOLO, L.2023-01-06T18:01:18Z2023-01-06T18:01:18Z2023-01-062022info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlePharmaceuticals, v. 15, n. 6, article 724, 2022.http://www.alice.cnptia.embrapa.br/alice/handle/doc/1150743https://doi.org/10.3390/ph15060724enginfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)instname:Empresa Brasileira de Pesquisa Agropecuária (Embrapa)instacron:EMBRAPA2023-01-06T18:01:18Zoai:www.alice.cnptia.embrapa.br:doc/1150743Repositório InstitucionalPUBhttps://www.alice.cnptia.embrapa.br/oai/requestopendoar:21542023-01-06T18:01:18falseRepositório InstitucionalPUBhttps://www.alice.cnptia.embrapa.br/oai/requestcg-riaa@embrapa.bropendoar:21542023-01-06T18:01:18Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) - Empresa Brasileira de Pesquisa Agropecuária (Embrapa)false
dc.title.none.fl_str_mv Purification, characterization and evaluation of the antitumoral activity of a phospholipase A2 from the snake Bothrops moojeni.
title Purification, characterization and evaluation of the antitumoral activity of a phospholipase A2 from the snake Bothrops moojeni.
spellingShingle Purification, characterization and evaluation of the antitumoral activity of a phospholipase A2 from the snake Bothrops moojeni.
FRIHLING, B. E. F.
Biotecnologia
Espectrometria
Proteína
Animal proteins
Biotechnology
Bothrops
Cell membranes
Mass spectrometry
Phospholipase A2
title_short Purification, characterization and evaluation of the antitumoral activity of a phospholipase A2 from the snake Bothrops moojeni.
title_full Purification, characterization and evaluation of the antitumoral activity of a phospholipase A2 from the snake Bothrops moojeni.
title_fullStr Purification, characterization and evaluation of the antitumoral activity of a phospholipase A2 from the snake Bothrops moojeni.
title_full_unstemmed Purification, characterization and evaluation of the antitumoral activity of a phospholipase A2 from the snake Bothrops moojeni.
title_sort Purification, characterization and evaluation of the antitumoral activity of a phospholipase A2 from the snake Bothrops moojeni.
author FRIHLING, B. E. F.
author_facet FRIHLING, B. E. F.
BOLETI, A. P. de A.
OLIVEIRA, C. F. R. de
SANCHES, S. C.
CARDOSO, P. H. de O.
VERBISCK, N. V.
MACEDO, M. L. R.
SANTA RITA, P. H.
CARVALHO, C. M. E.
MIGLIOLO, L.
author_role author
author2 BOLETI, A. P. de A.
OLIVEIRA, C. F. R. de
SANCHES, S. C.
CARDOSO, P. H. de O.
VERBISCK, N. V.
MACEDO, M. L. R.
SANTA RITA, P. H.
CARVALHO, C. M. E.
MIGLIOLO, L.
author2_role author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv BRENO 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.
dc.contributor.author.fl_str_mv FRIHLING, B. E. F.
BOLETI, A. P. de A.
OLIVEIRA, C. F. R. de
SANCHES, S. C.
CARDOSO, P. H. de O.
VERBISCK, N. V.
MACEDO, M. L. R.
SANTA RITA, P. H.
CARVALHO, C. M. E.
MIGLIOLO, L.
dc.subject.por.fl_str_mv Biotecnologia
Espectrometria
Proteína
Animal proteins
Biotechnology
Bothrops
Cell membranes
Mass spectrometry
Phospholipase A2
topic Biotecnologia
Espectrometria
Proteína
Animal proteins
Biotechnology
Bothrops
Cell membranes
Mass spectrometry
Phospholipase A2
description Nature 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.
publishDate 2022
dc.date.none.fl_str_mv 2022
2023-01-06T18:01:18Z
2023-01-06T18:01:18Z
2023-01-06
dc.type.driver.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv Pharmaceuticals, v. 15, n. 6, article 724, 2022.
http://www.alice.cnptia.embrapa.br/alice/handle/doc/1150743
https://doi.org/10.3390/ph15060724
identifier_str_mv Pharmaceuticals, v. 15, n. 6, article 724, 2022.
url http://www.alice.cnptia.embrapa.br/alice/handle/doc/1150743
https://doi.org/10.3390/ph15060724
dc.language.iso.fl_str_mv eng
language eng
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
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instname:Empresa Brasileira de Pesquisa Agropecuária (Embrapa)
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collection Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)
repository.name.fl_str_mv Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) - Empresa Brasileira de Pesquisa Agropecuária (Embrapa)
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