Isolation and biochemical characterization of bradykinin-potentiating peptides from Bitis gabonica rhinoceros
Abstract 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) inhibito...
Published in: | Journal of Venomous Animals and Toxins including Tropical Diseases |
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ftdoajarticles:oai:doaj.org/article:5f6dc3e710e34216a1648b094d2413d9 2023-05-15T15:11:42+02:00 Isolation and biochemical characterization of bradykinin-potentiating peptides from Bitis gabonica rhinoceros Tamara M. Fucase Juliana M. Sciani Ingrid Cavalcante Vincent L. Viala Bruno B. Chagas Daniel C. Pimenta Patrick J. Spencer 2017-06-01T00:00:00Z https://doi.org/10.1186/s40409-017-0124-9 https://doaj.org/article/5f6dc3e710e34216a1648b094d2413d9 EN eng SciELO http://link.springer.com/article/10.1186/s40409-017-0124-9 https://doaj.org/toc/1678-9199 doi:10.1186/s40409-017-0124-9 1678-9199 https://doaj.org/article/5f6dc3e710e34216a1648b094d2413d9 Journal of Venomous Animals and Toxins including Tropical Diseases, Vol 23, Iss 1, Pp 1-8 (2017) Peptide Hypotension Viperinae Arctic medicine. Tropical medicine RC955-962 Toxicology. Poisons RA1190-1270 Zoology QL1-991 article 2017 ftdoajarticles https://doi.org/10.1186/s40409-017-0124-9 2022-12-31T03:39:39Z Abstract 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. Article in Journal/Newspaper Arctic Directory of Open Access Journals: DOAJ Articles Arctic Journal of Venomous Animals and Toxins including Tropical Diseases 23 1 |
institution |
Open Polar |
collection |
Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
Peptide Hypotension Viperinae Arctic medicine. Tropical medicine RC955-962 Toxicology. Poisons RA1190-1270 Zoology QL1-991 |
spellingShingle |
Peptide Hypotension Viperinae Arctic medicine. Tropical medicine RC955-962 Toxicology. Poisons RA1190-1270 Zoology QL1-991 Tamara M. Fucase Juliana M. Sciani Ingrid Cavalcante Vincent L. Viala Bruno B. Chagas Daniel C. Pimenta Patrick J. Spencer Isolation and biochemical characterization of bradykinin-potentiating peptides from Bitis gabonica rhinoceros |
topic_facet |
Peptide Hypotension Viperinae Arctic medicine. Tropical medicine RC955-962 Toxicology. Poisons RA1190-1270 Zoology QL1-991 |
description |
Abstract 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. |
format |
Article in Journal/Newspaper |
author |
Tamara M. Fucase Juliana M. Sciani Ingrid Cavalcante Vincent L. Viala Bruno B. Chagas Daniel C. Pimenta Patrick J. Spencer |
author_facet |
Tamara M. Fucase Juliana M. Sciani Ingrid Cavalcante Vincent L. Viala Bruno B. Chagas Daniel C. Pimenta Patrick J. Spencer |
author_sort |
Tamara M. Fucase |
title |
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_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_sort |
isolation and biochemical characterization of bradykinin-potentiating peptides from bitis gabonica rhinoceros |
publisher |
SciELO |
publishDate |
2017 |
url |
https://doi.org/10.1186/s40409-017-0124-9 https://doaj.org/article/5f6dc3e710e34216a1648b094d2413d9 |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic |
genre_facet |
Arctic |
op_source |
Journal of Venomous Animals and Toxins including Tropical Diseases, Vol 23, Iss 1, Pp 1-8 (2017) |
op_relation |
http://link.springer.com/article/10.1186/s40409-017-0124-9 https://doaj.org/toc/1678-9199 doi:10.1186/s40409-017-0124-9 1678-9199 https://doaj.org/article/5f6dc3e710e34216a1648b094d2413d9 |
op_doi |
https://doi.org/10.1186/s40409-017-0124-9 |
container_title |
Journal of Venomous Animals and Toxins including Tropical Diseases |
container_volume |
23 |
container_issue |
1 |
_version_ |
1766342512611426304 |