Potent and Broad-Spectrum Antimicrobial Activity of Analogs from the Scorpion Peptide Stigmurin
Autor(a) principal: | |
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Data de Publicação: | 2019 |
Outros Autores: | , , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10362/116701 |
Resumo: | Scorpion venom constitutes a rich source of biologically active compounds with high potential for therapeutic and biotechnological applications that can be used as prototypes for the design of new drugs. The aim of this study was to characterize the structural conformation, evaluate the antimicrobial activity, and gain insight into the possible action mechanism underlying it, for two new analog peptides of the scorpion peptide Stigmurin, named StigA25 and StigA31. The amino acid substitutions in the native sequence for lysine residues resulted in peptides with higher positive net charge and hydrophobicity, with an increase in the theoretical helical content. StigA25 and StigA31 showed the capacity to modify their structural conformation according to the environment, and were stable to pH and temperature variation-results similar to the native peptide. Both analog peptides demonstrated broad-spectrum antimicrobial activity in vitro, showing an effect superior to that of the native peptide, being non-hemolytic at the biologically active concentrations. Therefore, this study demonstrates the therapeutic potential of the analog peptides from Stigmurin and the promising approach of rational drug design based on scorpion venom peptide to obtain new anti-infective agents. |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Potent and Broad-Spectrum Antimicrobial Activity of Analogs from the Scorpion Peptide StigmurinTityus stigmurusAnalog peptidesAntimicrobial agentsBacterial membraneMolecular dynamicsScorpion venomScorpion venom constitutes a rich source of biologically active compounds with high potential for therapeutic and biotechnological applications that can be used as prototypes for the design of new drugs. The aim of this study was to characterize the structural conformation, evaluate the antimicrobial activity, and gain insight into the possible action mechanism underlying it, for two new analog peptides of the scorpion peptide Stigmurin, named StigA25 and StigA31. The amino acid substitutions in the native sequence for lysine residues resulted in peptides with higher positive net charge and hydrophobicity, with an increase in the theoretical helical content. StigA25 and StigA31 showed the capacity to modify their structural conformation according to the environment, and were stable to pH and temperature variation-results similar to the native peptide. Both analog peptides demonstrated broad-spectrum antimicrobial activity in vitro, showing an effect superior to that of the native peptide, being non-hemolytic at the biologically active concentrations. Therefore, this study demonstrates the therapeutic potential of the analog peptides from Stigmurin and the promising approach of rational drug design based on scorpion venom peptide to obtain new anti-infective agents.Instituto de Higiene e Medicina Tropical (IHMT)Global Health and Tropical Medicine (GHTM)Vector borne diseases and pathogens (VBD)RUNBruno, Amorim-Carmo,Alessandra, Daniele-Silva,Adriana M.S., Parente,Allanny Alves, Furtado,Enéas De, Carvalho,Johny W.F., Oliveira,Elizabeth Cristina Gomes, Santos,Silva, MSSérgio R.B., Silva,Arnóbio Antônio Da, Silva-Júnior,Norberto K., Monteiro,Matheus De Freitas, Fernandes-Pedrosa,2021-05-02T22:41:03Z2019-01-312019-01-31T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article21application/pdfhttp://hdl.handle.net/10362/116701eng1422-0067PURE: 11658294https://doi.org/10.3390/ijms20030623info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-05-22T17:52:33Zoai:run.unl.pt:10362/116701Portal AgregadorONGhttps://www.rcaap.pt/oai/openairemluisa.alvim@gmail.comopendoar:71602024-05-22T17:52:33Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Potent and Broad-Spectrum Antimicrobial Activity of Analogs from the Scorpion Peptide Stigmurin |
title |
Potent and Broad-Spectrum Antimicrobial Activity of Analogs from the Scorpion Peptide Stigmurin |
spellingShingle |
Potent and Broad-Spectrum Antimicrobial Activity of Analogs from the Scorpion Peptide Stigmurin Bruno, Amorim-Carmo, Tityus stigmurus Analog peptides Antimicrobial agents Bacterial membrane Molecular dynamics Scorpion venom |
title_short |
Potent and Broad-Spectrum Antimicrobial Activity of Analogs from the Scorpion Peptide Stigmurin |
title_full |
Potent and Broad-Spectrum Antimicrobial Activity of Analogs from the Scorpion Peptide Stigmurin |
title_fullStr |
Potent and Broad-Spectrum Antimicrobial Activity of Analogs from the Scorpion Peptide Stigmurin |
title_full_unstemmed |
Potent and Broad-Spectrum Antimicrobial Activity of Analogs from the Scorpion Peptide Stigmurin |
title_sort |
Potent and Broad-Spectrum Antimicrobial Activity of Analogs from the Scorpion Peptide Stigmurin |
author |
Bruno, Amorim-Carmo, |
author_facet |
Bruno, Amorim-Carmo, Alessandra, Daniele-Silva, Adriana M.S., Parente, Allanny Alves, Furtado, Enéas De, Carvalho, Johny W.F., Oliveira, Elizabeth Cristina Gomes, Santos, Silva, MS Sérgio R.B., Silva, Arnóbio Antônio Da, Silva-Júnior, Norberto K., Monteiro, Matheus De Freitas, Fernandes-Pedrosa, |
author_role |
author |
author2 |
Alessandra, Daniele-Silva, Adriana M.S., Parente, Allanny Alves, Furtado, Enéas De, Carvalho, Johny W.F., Oliveira, Elizabeth Cristina Gomes, Santos, Silva, MS Sérgio R.B., Silva, Arnóbio Antônio Da, Silva-Júnior, Norberto K., Monteiro, Matheus De Freitas, Fernandes-Pedrosa, |
author2_role |
author author author author author author author author author author author |
dc.contributor.none.fl_str_mv |
Instituto de Higiene e Medicina Tropical (IHMT) Global Health and Tropical Medicine (GHTM) Vector borne diseases and pathogens (VBD) RUN |
dc.contributor.author.fl_str_mv |
Bruno, Amorim-Carmo, Alessandra, Daniele-Silva, Adriana M.S., Parente, Allanny Alves, Furtado, Enéas De, Carvalho, Johny W.F., Oliveira, Elizabeth Cristina Gomes, Santos, Silva, MS Sérgio R.B., Silva, Arnóbio Antônio Da, Silva-Júnior, Norberto K., Monteiro, Matheus De Freitas, Fernandes-Pedrosa, |
dc.subject.por.fl_str_mv |
Tityus stigmurus Analog peptides Antimicrobial agents Bacterial membrane Molecular dynamics Scorpion venom |
topic |
Tityus stigmurus Analog peptides Antimicrobial agents Bacterial membrane Molecular dynamics Scorpion venom |
description |
Scorpion venom constitutes a rich source of biologically active compounds with high potential for therapeutic and biotechnological applications that can be used as prototypes for the design of new drugs. The aim of this study was to characterize the structural conformation, evaluate the antimicrobial activity, and gain insight into the possible action mechanism underlying it, for two new analog peptides of the scorpion peptide Stigmurin, named StigA25 and StigA31. The amino acid substitutions in the native sequence for lysine residues resulted in peptides with higher positive net charge and hydrophobicity, with an increase in the theoretical helical content. StigA25 and StigA31 showed the capacity to modify their structural conformation according to the environment, and were stable to pH and temperature variation-results similar to the native peptide. Both analog peptides demonstrated broad-spectrum antimicrobial activity in vitro, showing an effect superior to that of the native peptide, being non-hemolytic at the biologically active concentrations. Therefore, this study demonstrates the therapeutic potential of the analog peptides from Stigmurin and the promising approach of rational drug design based on scorpion venom peptide to obtain new anti-infective agents. |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019-01-31 2019-01-31T00:00:00Z 2021-05-02T22:41:03Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10362/116701 |
url |
http://hdl.handle.net/10362/116701 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
1422-0067 PURE: 11658294 https://doi.org/10.3390/ijms20030623 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
21 application/pdf |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
repository.mail.fl_str_mv |
mluisa.alvim@gmail.com |
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1817545795481632768 |