The modular nature of bradykinin-potentiating peptides isolated from snake venoms

Detalhes bibliográficos
Autor(a) principal: Sciani,Juliana Mozer
Data de Publicação: 2017
Outros Autores: Pimenta,Daniel Carvalho
Tipo de documento: Artigo
Idioma: eng
Título da fonte: The Journal of venomous animals and toxins including tropical diseases (Online)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992017000100208
Resumo: Abstract Bradykinin-potentiating peptides (BPPs) are molecules discovered by Sergio Ferreira – who found them in the venom of Bothrops jararaca in the 1960s – that literally potentiate the action of bradykinin in vivo by, allegedly, inhibiting the angiotensin-converting enzymes. After administration, the global physiological effect of BPP is the decrease of the blood pressure. Due to this interesting effect, one of these peptides was used by David Cushman and Miguel Ondetti to develop a hypotensive drug, the widely known captopril, vastly employed on hypertension treatment. From that time on, many studies on BPPs have been conducted, basically describing new peptides and assaying their pharmacological effects, mostly in comparison to captopryl. After compiling most of these data, we are proposing that snake BPPs are ‘modular’ peptidic molecules, in which the combination of given amino acid ‘blocks’ results in the different existing peptides (BPPs), commonly found in snake venom. We have observed that there would be mandatory modules (present in all snake BPPs), such as the N-terminal pyroglutamic acid and C-terminal QIPP, and optionalmodules (amino acid blocks present in some of them), such as AP or WAQ. Scattered between these modules, there might be other amino acids that would ‘complete’ the peptide, without disrupting the signature of the classical BPP. This modular arrangement would represent an important evolutionary advantage in terms of biological diversity that might have its origins either at the genomic or at the post-translational modification levels. Regardless of the modules’ origin, the increase in the diversity of peptides has definitely been essential for snakes’ success on nature.
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spelling The modular nature of bradykinin-potentiating peptides isolated from snake venomsBothrops jararacaVenomSnake venomBradykinin-potentiating peptidesBPPModulesAbstract Bradykinin-potentiating peptides (BPPs) are molecules discovered by Sergio Ferreira – who found them in the venom of Bothrops jararaca in the 1960s – that literally potentiate the action of bradykinin in vivo by, allegedly, inhibiting the angiotensin-converting enzymes. After administration, the global physiological effect of BPP is the decrease of the blood pressure. Due to this interesting effect, one of these peptides was used by David Cushman and Miguel Ondetti to develop a hypotensive drug, the widely known captopril, vastly employed on hypertension treatment. From that time on, many studies on BPPs have been conducted, basically describing new peptides and assaying their pharmacological effects, mostly in comparison to captopryl. After compiling most of these data, we are proposing that snake BPPs are ‘modular’ peptidic molecules, in which the combination of given amino acid ‘blocks’ results in the different existing peptides (BPPs), commonly found in snake venom. We have observed that there would be mandatory modules (present in all snake BPPs), such as the N-terminal pyroglutamic acid and C-terminal QIPP, and optionalmodules (amino acid blocks present in some of them), such as AP or WAQ. Scattered between these modules, there might be other amino acids that would ‘complete’ the peptide, without disrupting the signature of the classical BPP. This modular arrangement would represent an important evolutionary advantage in terms of biological diversity that might have its origins either at the genomic or at the post-translational modification levels. Regardless of the modules’ origin, the increase in the diversity of peptides has definitely been essential for snakes’ success on nature.Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP)2017-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992017000100208Journal of Venomous Animals and Toxins including Tropical Diseases v.23 2017reponame:The Journal of venomous animals and toxins including tropical diseases (Online)instname:Universidade Estadual Paulista (UNESP)instacron:UNESP10.1186/s40409-017-0134-7info:eu-repo/semantics/openAccessSciani,Juliana MozerPimenta,Daniel Carvalhoeng2017-11-16T00:00:00Zoai:scielo:S1678-91992017000100208Revistahttp://www.scielo.br/jvatitdPUBhttps://old.scielo.br/oai/scielo-oai.php||editorial@jvat.org.br1678-91991678-9180opendoar:2017-11-16T00:00The Journal of venomous animals and toxins including tropical diseases (Online) - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv The modular nature of bradykinin-potentiating peptides isolated from snake venoms
title The modular nature of bradykinin-potentiating peptides isolated from snake venoms
spellingShingle The modular nature of bradykinin-potentiating peptides isolated from snake venoms
Sciani,Juliana Mozer
Bothrops jararaca
Venom
Snake venom
Bradykinin-potentiating peptides
BPP
Modules
title_short The modular nature of bradykinin-potentiating peptides isolated from snake venoms
title_full The modular nature of bradykinin-potentiating peptides isolated from snake venoms
title_fullStr The modular nature of bradykinin-potentiating peptides isolated from snake venoms
title_full_unstemmed The modular nature of bradykinin-potentiating peptides isolated from snake venoms
title_sort The modular nature of bradykinin-potentiating peptides isolated from snake venoms
author Sciani,Juliana Mozer
author_facet Sciani,Juliana Mozer
Pimenta,Daniel Carvalho
author_role author
author2 Pimenta,Daniel Carvalho
author2_role author
dc.contributor.author.fl_str_mv Sciani,Juliana Mozer
Pimenta,Daniel Carvalho
dc.subject.por.fl_str_mv Bothrops jararaca
Venom
Snake venom
Bradykinin-potentiating peptides
BPP
Modules
topic Bothrops jararaca
Venom
Snake venom
Bradykinin-potentiating peptides
BPP
Modules
description Abstract Bradykinin-potentiating peptides (BPPs) are molecules discovered by Sergio Ferreira – who found them in the venom of Bothrops jararaca in the 1960s – that literally potentiate the action of bradykinin in vivo by, allegedly, inhibiting the angiotensin-converting enzymes. After administration, the global physiological effect of BPP is the decrease of the blood pressure. Due to this interesting effect, one of these peptides was used by David Cushman and Miguel Ondetti to develop a hypotensive drug, the widely known captopril, vastly employed on hypertension treatment. From that time on, many studies on BPPs have been conducted, basically describing new peptides and assaying their pharmacological effects, mostly in comparison to captopryl. After compiling most of these data, we are proposing that snake BPPs are ‘modular’ peptidic molecules, in which the combination of given amino acid ‘blocks’ results in the different existing peptides (BPPs), commonly found in snake venom. We have observed that there would be mandatory modules (present in all snake BPPs), such as the N-terminal pyroglutamic acid and C-terminal QIPP, and optionalmodules (amino acid blocks present in some of them), such as AP or WAQ. Scattered between these modules, there might be other amino acids that would ‘complete’ the peptide, without disrupting the signature of the classical BPP. This modular arrangement would represent an important evolutionary advantage in terms of biological diversity that might have its origins either at the genomic or at the post-translational modification levels. Regardless of the modules’ origin, the increase in the diversity of peptides has definitely been essential for snakes’ success on nature.
publishDate 2017
dc.date.none.fl_str_mv 2017-01-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992017000100208
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992017000100208
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1186/s40409-017-0134-7
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP)
publisher.none.fl_str_mv Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP)
dc.source.none.fl_str_mv Journal of Venomous Animals and Toxins including Tropical Diseases v.23 2017
reponame:The Journal of venomous animals and toxins including tropical diseases (Online)
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str The Journal of venomous animals and toxins including tropical diseases (Online)
collection The Journal of venomous animals and toxins including tropical diseases (Online)
repository.name.fl_str_mv The Journal of venomous animals and toxins including tropical diseases (Online) - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv ||editorial@jvat.org.br
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