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Isolation and biochemical characterization of bradykinin-potentiating peptides from Bitis gabonica rhinoceros.
Fucase, Tamara M; Sciani, Juliana M; Cavalcante, Ingrid; Viala, Vincent L; Chagas, Bruno B; Pimenta, Daniel C; Spencer, Patrick J.
Afiliação
  • Fucase TM; Biotechnology Center, Nuclear and Energy Research Institute (IPEN), Av. Lineu Prestes, 2242, São Paulo, SP CEP 05508-000 Brazil.
  • Sciani JM; Laboratory of Biochemistry and Biophysics, Butantan Institute, Av. Vital Brasil, 1500, São Paulo, SP CEP 05503-900 Brazil.
  • Cavalcante I; Laboratory of Biochemistry and Biophysics, Butantan Institute, Av. Vital Brasil, 1500, São Paulo, SP CEP 05503-900 Brazil.
  • Viala VL; Biotechnology Center, Nuclear and Energy Research Institute (IPEN), Av. Lineu Prestes, 2242, São Paulo, SP CEP 05508-000 Brazil.
  • Chagas BB; Biotechnology Center, Nuclear and Energy Research Institute (IPEN), Av. Lineu Prestes, 2242, São Paulo, SP CEP 05508-000 Brazil.
  • Pimenta DC; Laboratory of Biochemistry and Biophysics, Butantan Institute, Av. Vital Brasil, 1500, São Paulo, SP CEP 05503-900 Brazil.
  • Spencer PJ; Biotechnology Center, Nuclear and Energy Research Institute (IPEN), Av. Lineu Prestes, 2242, São Paulo, SP CEP 05508-000 Brazil.
J Venom Anim Toxins Incl Trop Dis ; 23: 33, 2017.
Article em En | MEDLINE | ID: mdl-28670326
BACKGROUND: Venoms represent a still underexplored reservoir of bioactive components that might mitigate or cure diseases in conditions in which conventional therapy is ineffective. The bradykinin-potentiating peptides (BPPs) comprise a class of angiotensin-I converting enzyme (ACE) inhibitors. The BPPs usually consist of oligopeptides with 5 to 13 residues with a high number of proline residues and the tripeptide Ile-Pro-Pro (IPP-tripeptide) in the C-terminus region and have a conserved N-terminal pyroglutamate residue. As a whole, the action of the BPPs on prey and snakebite victims results in the decrease of the blood pressure. The aim of this work was to isolate and characterize novel BPPs from the venom of Bitis gabonica rhinoceros. METHODS: The crude venom of B. g. rhinoceros was fractionated by size exclusion chromatography and the peptide fraction (<7 kDa) was separated by reverse phase chromatography (RP-HPLC) and analyzed by ESI-IT-TOF-MS/MS. One new BPP was identified, synthetized and assayed for ACE inhibition and, in vivo, for edema potentiation. RESULTS: Typical BPP signatures were identified in three RP-HPLC fractions. CID fragmentation presented the usual y-ion of the terminal P-P fragment as a predominant signal at m/z 213.1. De novo peptide sequencing identified one Bothrops-like BPP and one new BPP sequence. The new BPP was synthesized and showed poor inhibition over ACE, but displayed significant bradykinin-induced edema potentiation. CONCLUSIONS: So far, few BPPs are described in Viperinae, and based on the sequenced peptides, two non-canonical sequences were detected. The possible clinical role of this new peptides remains unclear.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: J Venom Anim Toxins Incl Trop Dis Ano de publicação: 2017 Tipo de documento: Article País de publicação: Brasil
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: J Venom Anim Toxins Incl Trop Dis Ano de publicação: 2017 Tipo de documento: Article País de publicação: Brasil