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Isolation and biochemical characterization of bradykinin-potentiating peptides from Bitis gabonica rhinoceros

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...

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Autores principales: Fucase, Tamara M., Sciani, Juliana M., Cavalcante, Ingrid, Viala, Vincent L., Chagas, Bruno B., Pimenta, Daniel C., Spencer, Patrick J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5485657/
https://www.ncbi.nlm.nih.gov/pubmed/28670326
http://dx.doi.org/10.1186/s40409-017-0124-9
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author Fucase, Tamara M.
Sciani, Juliana M.
Cavalcante, Ingrid
Viala, Vincent L.
Chagas, Bruno B.
Pimenta, Daniel C.
Spencer, Patrick J.
author_facet Fucase, Tamara M.
Sciani, Juliana M.
Cavalcante, Ingrid
Viala, Vincent L.
Chagas, Bruno B.
Pimenta, Daniel C.
Spencer, Patrick J.
author_sort Fucase, Tamara M.
collection PubMed
description 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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spelling pubmed-54856572017-06-30 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. J Venom Anim Toxins Incl Trop Dis Research 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. BioMed Central 2017-06-26 /pmc/articles/PMC5485657/ /pubmed/28670326 http://dx.doi.org/10.1186/s40409-017-0124-9 Text en © The Author(s). 2017 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research
Fucase, Tamara M.
Sciani, Juliana M.
Cavalcante, Ingrid
Viala, Vincent L.
Chagas, Bruno B.
Pimenta, Daniel C.
Spencer, Patrick J.
Isolation and biochemical characterization of bradykinin-potentiating peptides from Bitis gabonica rhinoceros
title Isolation and biochemical characterization of bradykinin-potentiating peptides from Bitis gabonica rhinoceros
title_full Isolation and biochemical characterization of bradykinin-potentiating peptides from Bitis gabonica rhinoceros
title_fullStr Isolation and biochemical characterization of bradykinin-potentiating peptides from Bitis gabonica rhinoceros
title_full_unstemmed Isolation and biochemical characterization of bradykinin-potentiating peptides from Bitis gabonica rhinoceros
title_short Isolation and biochemical characterization of bradykinin-potentiating peptides from Bitis gabonica rhinoceros
title_sort isolation and biochemical characterization of bradykinin-potentiating peptides from bitis gabonica rhinoceros
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5485657/
https://www.ncbi.nlm.nih.gov/pubmed/28670326
http://dx.doi.org/10.1186/s40409-017-0124-9
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