Potent and Broad-Spectrum Antimicrobial Activity of Analogs from the Scorpion Peptide Stigmurin

Detalhes bibliográficos
Autor(a) principal: Bruno, Amorim-Carmo
Data de Publicação: 2019
Outros Autores: 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
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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spelling 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:RCAAP2024-03-11T04:59:23Zoai:run.unl.pt:10362/116701Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:43:12.963581Repositório 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
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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
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