Title:	Purification, characterization and evaluation of the antitumoral activity of a phospholipase A2 from the snake Bothrops moojeni.
Authors:	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.
Affiliation:	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.
Date Issued:	2022
Citation:	Pharmaceuticals, v. 15, n. 6, article 724, 2022.
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.
Thesagro:	Biotecnologia Espectrometria Proteína
NAL Thesaurus:	Animal proteins Biotechnology Bothrops Cell membranes Mass spectrometry Phospholipase A2
DOI:	https://doi.org/10.3390/ph15060724
Notes:	Na publicação: Newton Verbisck.
Type of Material:	Artigo de periódico
Access:	openAccess
Appears in Collections:	Artigo em periódico indexado (CNPGC)