Biological activity of antibacterial peptides matches synergism between electrostatic and non electrostatic forces

Detalhes bibliográficos
Autor(a) principal: Bouchet, Ana M.
Data de Publicação: 2014
Outros Autores: Iannucci, Nancy B., Pastrian, María B., Cascone, Osvaldo, Santos, Nuno C., Disalvo, Edgardo A., Hollmann, Axel
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10451/23536
Resumo: © 2013 Elsevier B.V. All rights reserved.
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spelling Biological activity of antibacterial peptides matches synergism between electrostatic and non electrostatic forcesAntimicrobial peptideLysozymePeptide–membrane interactionsHydrophilic–hydrophobic synergism© 2013 Elsevier B.V. All rights reserved.Substitution of Ala 108 and Ala 111 in the 107–115 human lysozyme (hLz) fragment results in a 20-fold increased anti-staphylococcal activity while its hemolytic activity becomes significant (30%) at veryhigh concentrations. This analog displays an additional positive charge near the N-terminus (108) and anextra Trp residue at the center of the molecule (111), indicating that this particular amino acid sequenceimproves its interaction with the bacterial plasma membrane. In order to understand the role of thisarrangement in the membrane interaction, studies with model lipid membranes were carried out.The interactions of peptides, 107–115 hLz and the novel analog ([K108W111]107–115 hLz) with lipo-somes and lipid monolayers were evaluated by monitoring the changes in the fluorescence of the Trpresidues and the variation of the monolayers surface pressure, respectively. Results obtained with bothtechniques revealed a significant affinity increase of [K108W111]107–115 hLz for lipids, especially whenthe membranes containing negatively charged lipids, such as phosphatidylglycerol. However, there is alsoa significant interaction with zwitterionic lipids, suggesting that other forces in addition to electrostaticinteractions are involved in the binding. The analysis of adsorption isotherms and the insertion kineticssuggest that relaxation processes of the membrane structure are involved in the insertion process ofnovel peptide [K108W111]107–115 hLz but not in 107–115 hLz, probably by imposing a reorganization ofwater at the interphases.In this regard, the enhanced activity of peptide [K108W111]107–115 hLz may be explained by a syner-gistic effect between the increased electrostatic forces as well as the increased hydrophobic interactions.This work was supported with funds from Agencia Nacional de Promoción Cientiífica y Tecnológica, PICT 2007-757, PICT 2011-2606, CONICET (PIP 2011-2013 GI 11220100100484), UBACyT (20020090200663), (Programa-UNSE 23/A164), Fundação para a Ciência e a Tecnologia—Ministério da Educação e Ciência (FCT-MEC, Portugal), and FP7-PEOPLE IRSES (International Research Staff Exchange Scheme, European Union) project MEMPEPACROSS. EAD, NI, OC and AH are members of the Research Career of CONICET (Consejo Nacional de Investigaciones Científicas y Técnicas de la República Argentina). AB is recipient of a post doctoral fellowship of CONICET. AH is recipient of a post doctoral fellowship of FCT-MEC (SFRH/BPD/72037/2010). The authors thank Chemo-RomikinSA (Argentina) for use of their Peptide Synthesizer facilities.ElsevierRepositório da Universidade de LisboaBouchet, Ana M.Iannucci, Nancy B.Pastrian, María B.Cascone, OsvaldoSantos, Nuno C.Disalvo, Edgardo A.Hollmann, Axel2016-04-26T15:33:17Z20142014-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10451/23536engColloids and Surfaces B: Biointerfaces 114 (2014) 363– 3710927-776510.1016/j.colsurfb.2013.10.025metadata 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:RCAAP2023-11-08T16:11:36Zoai:repositorio.ul.pt:10451/23536Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T21:40:51.689441Repositório 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 Biological activity of antibacterial peptides matches synergism between electrostatic and non electrostatic forces
title Biological activity of antibacterial peptides matches synergism between electrostatic and non electrostatic forces
spellingShingle Biological activity of antibacterial peptides matches synergism between electrostatic and non electrostatic forces
Bouchet, Ana M.
Antimicrobial peptide
Lysozyme
Peptide–membrane interactions
Hydrophilic–hydrophobic synergism
title_short Biological activity of antibacterial peptides matches synergism between electrostatic and non electrostatic forces
title_full Biological activity of antibacterial peptides matches synergism between electrostatic and non electrostatic forces
title_fullStr Biological activity of antibacterial peptides matches synergism between electrostatic and non electrostatic forces
title_full_unstemmed Biological activity of antibacterial peptides matches synergism between electrostatic and non electrostatic forces
title_sort Biological activity of antibacterial peptides matches synergism between electrostatic and non electrostatic forces
author Bouchet, Ana M.
author_facet Bouchet, Ana M.
Iannucci, Nancy B.
Pastrian, María B.
Cascone, Osvaldo
Santos, Nuno C.
Disalvo, Edgardo A.
Hollmann, Axel
author_role author
author2 Iannucci, Nancy B.
Pastrian, María B.
Cascone, Osvaldo
Santos, Nuno C.
Disalvo, Edgardo A.
Hollmann, Axel
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 Bouchet, Ana M.
Iannucci, Nancy B.
Pastrian, María B.
Cascone, Osvaldo
Santos, Nuno C.
Disalvo, Edgardo A.
Hollmann, Axel
dc.subject.por.fl_str_mv Antimicrobial peptide
Lysozyme
Peptide–membrane interactions
Hydrophilic–hydrophobic synergism
topic Antimicrobial peptide
Lysozyme
Peptide–membrane interactions
Hydrophilic–hydrophobic synergism
description © 2013 Elsevier B.V. All rights reserved.
publishDate 2014
dc.date.none.fl_str_mv 2014
2014-01-01T00:00:00Z
2016-04-26T15:33:17Z
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/10451/23536
url http://hdl.handle.net/10451/23536
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Colloids and Surfaces B: Biointerfaces 114 (2014) 363– 371
0927-7765
10.1016/j.colsurfb.2013.10.025
dc.rights.driver.fl_str_mv metadata only access
info:eu-repo/semantics/openAccess
rights_invalid_str_mv metadata only access
eu_rights_str_mv openAccess
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
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
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