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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Isolation and characterization of a novel metalloprotease inhibitor from Bothrops alternatus snake serum

Texto completo
Autor(es):
Palacio, Tatiana Z. ; Santos-Filho, Norival A. ; Rosa, Jose Cesar ; Ferreira Junior, Rui S. ; Barraviera, Benedito ; Sampaio, Suely V.
Número total de Autores: 6
Tipo de documento: Artigo Científico
Fonte: International Journal of Biological Macromolecules; v. 98, p. 436-446, MAY 2017.
Citações Web of Science: 5
Resumo

Resistance of snakes and some other animals to snake envenomation has been attributed to soluble factors present in their tissues. Here we report the isolation of a novel metalloprotease inhibitor from Bothrops alternatus snake serum (named BaltMPI) with high purity, using a four-step chromatographic method. BaltMPI has molecular weights of 60.5 and 42.4 kDa, as determined by SDS-PAGE and mass spectrometry, respectively, and pI = 5.27. The first 60 amino acids from the N-terminal region of BaltMPI, determined by Edman's degradation, showed high homology (97%) with the snake venom metalloprotease inhibitor (SVMPI) BJ46a and other SVMPIs (78-82%). The chromatographic fractions and purified BaltMPl exhibited anti-hemorrhagic activity against Batroxase and BjussuMP-I. BaltMPl was stable over wide ranges of pH (1, 5, 8, and 9) and temperature (-80, 20, 4, 60, and 100 degrees C), and suppressed the fibrinogenolytic, fibrinolytic, and azocaseinolytic activities of Batroxase. BaltMPI specifically inhibited the activity of metalloproteases, without affecting the activity of serine proteases. Together, our results suggest that BaltMPl and other SVMPIs are promising molecules for the treatment of snake envenomation, in particular that caused by Bothrops sp. (C) 2017 Elsevier B.V. All rights reserved. (AU)

Processo FAPESP: 12/02734-9 - Isolamento e caracterização bioquímica e funcional de um inibidor de metaloproteases presente no soro da serpente Bothrops alternatus
Beneficiário:Tatiana Zapata Palacio
Modalidade de apoio: Bolsas no Brasil - Mestrado
Processo FAPESP: 11/23236-4 - Toxinas animais nativas e recombinantes: análise funcional, estrutural e molecular
Beneficiário:Suely Vilela
Modalidade de apoio: Auxílio à Pesquisa - Temático