Design and characterization of novel antimicrobial peptides, R-BP100 and RW-BP100, with activity against Gram-negative and Gram-positive bacteria

Detalhes bibliográficos
Autor(a) principal: Torcato, Inês M.
Data de Publicação: 2013
Outros Autores: Huang, Yen-Hua, Franquelim, Henri G., Gaspar, Diana, Craik, David J., Castanho, Miguel A. R. B., Henriques, Sónia Troeira
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10451/10694
Resumo: © 2012 Elsevier B.V. All rights reserved.
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spelling Design and characterization of novel antimicrobial peptides, R-BP100 and RW-BP100, with activity against Gram-negative and Gram-positive bacteriaAntimicrobial peptideModel membranePeptide–membrane interactionAtomic force microscopyTrp/Tyr fluorescence© 2012 Elsevier B.V. All rights reserved.BP100 is a short cationic antimicrobial peptide with a mechanism of action dependent on peptide–lipid interactions and microbial surface charge neutralization. Although active against Gram-negative bacteria, BP100 is inactive against Gram-positive bacteria. In this study we report two newly designed BP100 analogues, RW-BP100 and R-BP100 that have the Tyr residue replaced with a Trp and/or the Lys residues replaced with an Arg. The new analogues in addition to being active against Gram-negative bacteria, possess activity against all tested Gram-positive bacteria. Mechanistic studies using atomic force microscopy, surface plasmon resonance and fluorescence methodologies reveal that the antibacterial efficiency follows the affinity for bacterial membrane. The studies suggest that the activity of BP100 and its analogues against Gram-negative bacteria is mainly driven by electrostatic interactions with the lipopolysaccharide layer and is followed by binding to and disruption of the inner membrane, whereas activity against Gram-positive bacteria, in addition to electrostatic attraction to the exposed lipoteichoic acids, requires an ability to more deeply insert in the membrane environment, which is favoured with Arg residues and is facilitated in the presence of a Trp residue. Knowledge on the mechanism of action of these antimicrobial peptides provides information that assists in the design of antimicrobials with higher efficacy and broader spectra of action, but also on the design of peptides with higher specificity if required.IMT work was supported by a grant (PTDC/SAU-BEB/099142/2008), HGF and DG held a scholarship from the Fundação para a Ciência e Tecnologia, Portugal, SFRH/BD/39039/2007 and SFRH/BPD/73500/2010, respectively. STH is the recipient of a Discovery Early Career Researcher Award (DE120103152), awarded by Australian Research Council. DJC is a National Health and Medical Research Council Fellow. We thank Marta Ribeiro (IMM, Lisbon University) for the valuable scientific discussions. We thank Dr Mark Blaskovich (IMB, UQ) for kindly providing the bacterial strains employed in this study and Angela Kavanagh (IMB, UQ) for the help in establishing the antimicrobial assays.ElsevierRepositório da Universidade de LisboaTorcato, Inês M.Huang, Yen-HuaFranquelim, Henri G.Gaspar, DianaCraik, David J.Castanho, Miguel A. R. B.Henriques, Sónia Troeira2014-03-06T11:37:53Z20132013-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10451/10694engBiochimica et Biophysica Acta 1828 (2013) 944–9550006-3002metadata only accessinfo: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:RCAAP2023-11-08T15:56:21Zoai:repositorio.ul.pt:10451/10694Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T21:34:37.930099Repositório 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 Design and characterization of novel antimicrobial peptides, R-BP100 and RW-BP100, with activity against Gram-negative and Gram-positive bacteria
title Design and characterization of novel antimicrobial peptides, R-BP100 and RW-BP100, with activity against Gram-negative and Gram-positive bacteria
spellingShingle Design and characterization of novel antimicrobial peptides, R-BP100 and RW-BP100, with activity against Gram-negative and Gram-positive bacteria
Torcato, Inês M.
Antimicrobial peptide
Model membrane
Peptide–membrane interaction
Atomic force microscopy
Trp/Tyr fluorescence
title_short Design and characterization of novel antimicrobial peptides, R-BP100 and RW-BP100, with activity against Gram-negative and Gram-positive bacteria
title_full Design and characterization of novel antimicrobial peptides, R-BP100 and RW-BP100, with activity against Gram-negative and Gram-positive bacteria
title_fullStr Design and characterization of novel antimicrobial peptides, R-BP100 and RW-BP100, with activity against Gram-negative and Gram-positive bacteria
title_full_unstemmed Design and characterization of novel antimicrobial peptides, R-BP100 and RW-BP100, with activity against Gram-negative and Gram-positive bacteria
title_sort Design and characterization of novel antimicrobial peptides, R-BP100 and RW-BP100, with activity against Gram-negative and Gram-positive bacteria
author Torcato, Inês M.
author_facet Torcato, Inês M.
Huang, Yen-Hua
Franquelim, Henri G.
Gaspar, Diana
Craik, David J.
Castanho, Miguel A. R. B.
Henriques, Sónia Troeira
author_role author
author2 Huang, Yen-Hua
Franquelim, Henri G.
Gaspar, Diana
Craik, David J.
Castanho, Miguel A. R. B.
Henriques, Sónia Troeira
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Repositório da Universidade de Lisboa
dc.contributor.author.fl_str_mv Torcato, Inês M.
Huang, Yen-Hua
Franquelim, Henri G.
Gaspar, Diana
Craik, David J.
Castanho, Miguel A. R. B.
Henriques, Sónia Troeira
dc.subject.por.fl_str_mv Antimicrobial peptide
Model membrane
Peptide–membrane interaction
Atomic force microscopy
Trp/Tyr fluorescence
topic Antimicrobial peptide
Model membrane
Peptide–membrane interaction
Atomic force microscopy
Trp/Tyr fluorescence
description © 2012 Elsevier B.V. All rights reserved.
publishDate 2013
dc.date.none.fl_str_mv 2013
2013-01-01T00:00:00Z
2014-03-06T11:37:53Z
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/10451/10694
url http://hdl.handle.net/10451/10694
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Biochimica et Biophysica Acta 1828 (2013) 944–955
0006-3002
dc.rights.driver.fl_str_mv metadata only access
info:eu-repo/semantics/openAccess
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dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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
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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
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