Novel neuroprotective peptides in the venom of the solitary scoliid wasp Scolia decorata ventralis

Detalhes bibliográficos
Autor(a) principal: Alberto-Silva,Carlos
Data de Publicação: 2021
Outros Autores: Portaro,Fernanda Calheta Vieira, Kodama,Roberto Tadashi, Pantaleão,Halyne Queiroz, Rangel,Marisa, Nihei,Ken-ichi, Konno,Katsuhiro
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=S1678-91992021000100313
Resumo: Abstract Background Solitary wasp venoms may be a rich source of neuroactive substances, since their venoms are used for paralyzing preys. We have been exploring bioactive constituents of solitary wasp venoms and, in this study, the component profile of the venom from a solitary scoliid wasp, Scolia decorata ventralis, was investigated through a comprehensive analysis using LC-MS. Two peptides were synthesized, and their neuroprotective properties were evaluated. Methods A reverse-phase HPLC connected to ESI-MS was used for LC-MS analyses. Online mass fingerprinting was performed from TIC, and data-dependent tandem mass spectrometry gave the MS/MS spectra. The sequences of two major peptide components were determined by MALDI-TOF/TOF MS analysis, confirmed by solid phase synthesis. Using the synthetic peptides, biological activities were assessed. Cell integrity tests and neuroprotection analyzes using H2O2 as an oxidative stress inducer were performed for both peptides. Results Online mass fingerprinting revealed that the venom contains 123 components, and the MS/MS analysis resulted in 33 full sequences of peptide components. The two main peptides, α-scoliidine (DYVTVKGFSPLR) and β-scoliidine (DYVTVKGFSPLRKA), present homology with the bradykinin C-terminal. Despite this, both peptides did not behave as substrates or inhibitors of ACE, indicating that they do not interact with this metallopeptidase. In further studies, β-scoliidine, but not α -scoliidine, showed protective effects against oxidative stress-induced neurotoxicity in PC12 cells through integrity and metabolism cell assays. Interestingly, β-scoliidine has the extension of the KA dipeptide at the C-terminal in comparison with α-scoliidine. Conclusion Comprehensive LC-MS and MS/MS analyses from the Scolia decorata ventralis venom displayed the component profile of this venom. β-scoliidine showed an effective cytoprotective effect, probably due to the observed increase in the number of cells. This is the first report of solitary wasp venom peptides showing neuroprotective activity.
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spelling Novel neuroprotective peptides in the venom of the solitary scoliid wasp Scolia decorata ventralisComprehensive analysisLC-ESI-MSSolitary waspVenomNeuroprotective peptideAbstract Background Solitary wasp venoms may be a rich source of neuroactive substances, since their venoms are used for paralyzing preys. We have been exploring bioactive constituents of solitary wasp venoms and, in this study, the component profile of the venom from a solitary scoliid wasp, Scolia decorata ventralis, was investigated through a comprehensive analysis using LC-MS. Two peptides were synthesized, and their neuroprotective properties were evaluated. Methods A reverse-phase HPLC connected to ESI-MS was used for LC-MS analyses. Online mass fingerprinting was performed from TIC, and data-dependent tandem mass spectrometry gave the MS/MS spectra. The sequences of two major peptide components were determined by MALDI-TOF/TOF MS analysis, confirmed by solid phase synthesis. Using the synthetic peptides, biological activities were assessed. Cell integrity tests and neuroprotection analyzes using H2O2 as an oxidative stress inducer were performed for both peptides. Results Online mass fingerprinting revealed that the venom contains 123 components, and the MS/MS analysis resulted in 33 full sequences of peptide components. The two main peptides, α-scoliidine (DYVTVKGFSPLR) and β-scoliidine (DYVTVKGFSPLRKA), present homology with the bradykinin C-terminal. Despite this, both peptides did not behave as substrates or inhibitors of ACE, indicating that they do not interact with this metallopeptidase. In further studies, β-scoliidine, but not α -scoliidine, showed protective effects against oxidative stress-induced neurotoxicity in PC12 cells through integrity and metabolism cell assays. Interestingly, β-scoliidine has the extension of the KA dipeptide at the C-terminal in comparison with α-scoliidine. Conclusion Comprehensive LC-MS and MS/MS analyses from the Scolia decorata ventralis venom displayed the component profile of this venom. β-scoliidine showed an effective cytoprotective effect, probably due to the observed increase in the number of cells. This is the first report of solitary wasp venom peptides showing neuroprotective activity.Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP)2021-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992021000100313Journal of Venomous Animals and Toxins including Tropical Diseases v.27 2021reponame:The Journal of venomous animals and toxins including tropical diseases (Online)instname:Universidade Estadual Paulista (UNESP)instacron:UNESP10.1590/1678-9199-jvatitd-2020-0171info:eu-repo/semantics/openAccessAlberto-Silva,CarlosPortaro,Fernanda Calheta VieiraKodama,Roberto TadashiPantaleão,Halyne QueirozRangel,MarisaNihei,Ken-ichiKonno,Katsuhiroeng2021-06-08T00:00:00Zoai:scielo:S1678-91992021000100313Revistahttp://www.scielo.br/jvatitdPUBhttps://old.scielo.br/oai/scielo-oai.php||editorial@jvat.org.br1678-91991678-9180opendoar:2021-06-08T00:00The Journal of venomous animals and toxins including tropical diseases (Online) - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Novel neuroprotective peptides in the venom of the solitary scoliid wasp Scolia decorata ventralis
title Novel neuroprotective peptides in the venom of the solitary scoliid wasp Scolia decorata ventralis
spellingShingle Novel neuroprotective peptides in the venom of the solitary scoliid wasp Scolia decorata ventralis
Alberto-Silva,Carlos
Comprehensive analysis
LC-ESI-MS
Solitary wasp
Venom
Neuroprotective peptide
title_short Novel neuroprotective peptides in the venom of the solitary scoliid wasp Scolia decorata ventralis
title_full Novel neuroprotective peptides in the venom of the solitary scoliid wasp Scolia decorata ventralis
title_fullStr Novel neuroprotective peptides in the venom of the solitary scoliid wasp Scolia decorata ventralis
title_full_unstemmed Novel neuroprotective peptides in the venom of the solitary scoliid wasp Scolia decorata ventralis
title_sort Novel neuroprotective peptides in the venom of the solitary scoliid wasp Scolia decorata ventralis
author Alberto-Silva,Carlos
author_facet Alberto-Silva,Carlos
Portaro,Fernanda Calheta Vieira
Kodama,Roberto Tadashi
Pantaleão,Halyne Queiroz
Rangel,Marisa
Nihei,Ken-ichi
Konno,Katsuhiro
author_role author
author2 Portaro,Fernanda Calheta Vieira
Kodama,Roberto Tadashi
Pantaleão,Halyne Queiroz
Rangel,Marisa
Nihei,Ken-ichi
Konno,Katsuhiro
author2_role author
author
author
author
author
author
dc.contributor.author.fl_str_mv Alberto-Silva,Carlos
Portaro,Fernanda Calheta Vieira
Kodama,Roberto Tadashi
Pantaleão,Halyne Queiroz
Rangel,Marisa
Nihei,Ken-ichi
Konno,Katsuhiro
dc.subject.por.fl_str_mv Comprehensive analysis
LC-ESI-MS
Solitary wasp
Venom
Neuroprotective peptide
topic Comprehensive analysis
LC-ESI-MS
Solitary wasp
Venom
Neuroprotective peptide
description Abstract Background Solitary wasp venoms may be a rich source of neuroactive substances, since their venoms are used for paralyzing preys. We have been exploring bioactive constituents of solitary wasp venoms and, in this study, the component profile of the venom from a solitary scoliid wasp, Scolia decorata ventralis, was investigated through a comprehensive analysis using LC-MS. Two peptides were synthesized, and their neuroprotective properties were evaluated. Methods A reverse-phase HPLC connected to ESI-MS was used for LC-MS analyses. Online mass fingerprinting was performed from TIC, and data-dependent tandem mass spectrometry gave the MS/MS spectra. The sequences of two major peptide components were determined by MALDI-TOF/TOF MS analysis, confirmed by solid phase synthesis. Using the synthetic peptides, biological activities were assessed. Cell integrity tests and neuroprotection analyzes using H2O2 as an oxidative stress inducer were performed for both peptides. Results Online mass fingerprinting revealed that the venom contains 123 components, and the MS/MS analysis resulted in 33 full sequences of peptide components. The two main peptides, α-scoliidine (DYVTVKGFSPLR) and β-scoliidine (DYVTVKGFSPLRKA), present homology with the bradykinin C-terminal. Despite this, both peptides did not behave as substrates or inhibitors of ACE, indicating that they do not interact with this metallopeptidase. In further studies, β-scoliidine, but not α -scoliidine, showed protective effects against oxidative stress-induced neurotoxicity in PC12 cells through integrity and metabolism cell assays. Interestingly, β-scoliidine has the extension of the KA dipeptide at the C-terminal in comparison with α-scoliidine. Conclusion Comprehensive LC-MS and MS/MS analyses from the Scolia decorata ventralis venom displayed the component profile of this venom. β-scoliidine showed an effective cytoprotective effect, probably due to the observed increase in the number of cells. This is the first report of solitary wasp venom peptides showing neuroprotective activity.
publishDate 2021
dc.date.none.fl_str_mv 2021-01-01
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=S1678-91992021000100313
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992021000100313
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/1678-9199-jvatitd-2020-0171
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.27 2021
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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