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

Autores
Bouchet, Ana María; Iannucci, Nancy Beatriz; Pastrian, María Belén; Cascone, Osvaldo; Santos, Nuno C.; Disalvo, Edgardo Anibal; Hollmann, Axel
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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 very high concentrations. This analog displays an additional positive charge near the N-terminus (108) and an extra Trp residue at the center of the molecule (111), indicating that this particular amino acid sequence improves its interaction with the bacterial plasma membrane. In order to understand the role of this arrangement 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 liposomes and lipid monolayers were evaluated by monitoring the changes in the fluorescence of the Trp residues and the variation of the monolayers surface pressure, respectively. Results obtained with both techniques revealed a significant affinity increase of [K108W111]107–115 hLz for lipids, especially when the membranes containing negatively charged lipids, such as phosphatidylglycerol. However,there is also a significant interaction with zwitterionic lipids, suggesting that other forces in addition to electrostatic interactions are involved in the binding. The analysis of adsorption isotherms and the insertion kinetics suggest that relaxation processes of the membrane structure are involved in the insertion process of novel peptide [K108W111]107–115 hLz but not in 107–115 hLz, probably by imposing a reorganization of water at the interphases. In this regard, the enhanced activity of peptide [K108W111]107–115 hLz may be explained by a synergistic effect between the increased electrostatic forces as well as the increased hydrophobic interactions.
Fil: Bouchet, Ana María. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
Fil: Iannucci, Nancy Beatriz. Romikin S.a; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Microbiología, Inmunología y Biotecnología. Cátedra de Microbiología Industrial y Biotecnología; Argentina
Fil: Pastrian, María Belén. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Microbiología, Inmunología y Biotecnología. Cátedra de Microbiología Industrial y Biotecnología; Argentina
Fil: Cascone, Osvaldo. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Microbiología, Inmunología y Biotecnología. Cátedra de Microbiología Industrial y Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Santos, Nuno C.. Universidade Nova de Lisboa. Faculdade de Ciencias Medicas.; Portugal
Fil: Disalvo, Edgardo Anibal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
Fil: Hollmann, Axel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnologia. Instituto de Microbiologia Basica y Aplicada.; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina. Universidade Nova de Lisboa. Faculdade de Ciencias Medicas.; Portugal
Materia
ANTIMICROBIAL PEPTIDE
LYSOZYME
PEPTIDEMEMBRANE INTERACTION
HYDROPHILIC HYDROPHOBIC SYNERGISM
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/105284
Acceder
id CONICETDig_b541e2a7162ef9400b56f78c5949bb26
oai_identifier_str oai:ri.conicet.gov.ar:11336/105284
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Biological activity of antibacterial peptides matches synergism between electrostatic and non electrostatic forcesBouchet, Ana MaríaIannucci, Nancy BeatrizPastrian, María BelénCascone, OsvaldoSantos, Nuno C.Disalvo, Edgardo AnibalHollmann, AxelANTIMICROBIAL PEPTIDELYSOZYMEPEPTIDEMEMBRANE INTERACTIONHYDROPHILIC HYDROPHOBIC SYNERGISMhttps://purl.org/becyt/ford/3.4https://purl.org/becyt/ford/3Substitution 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 very high concentrations. This analog displays an additional positive charge near the N-terminus (108) and an extra Trp residue at the center of the molecule (111), indicating that this particular amino acid sequence improves its interaction with the bacterial plasma membrane. In order to understand the role of this arrangement 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 liposomes and lipid monolayers were evaluated by monitoring the changes in the fluorescence of the Trp residues and the variation of the monolayers surface pressure, respectively. Results obtained with both techniques revealed a significant affinity increase of [K108W111]107–115 hLz for lipids, especially when the membranes containing negatively charged lipids, such as phosphatidylglycerol. However,there is also a significant interaction with zwitterionic lipids, suggesting that other forces in addition to electrostatic interactions are involved in the binding. The analysis of adsorption isotherms and the insertion kinetics suggest that relaxation processes of the membrane structure are involved in the insertion process of novel peptide [K108W111]107–115 hLz but not in 107–115 hLz, probably by imposing a reorganization of water at the interphases. In this regard, the enhanced activity of peptide [K108W111]107–115 hLz may be explained by a synergistic effect between the increased electrostatic forces as well as the increased hydrophobic interactions.Fil: Bouchet, Ana María. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; ArgentinaFil: Iannucci, Nancy Beatriz. Romikin S.a; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Microbiología, Inmunología y Biotecnología. Cátedra de Microbiología Industrial y Biotecnología; ArgentinaFil: Pastrian, María Belén. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Microbiología, Inmunología y Biotecnología. Cátedra de Microbiología Industrial y Biotecnología; ArgentinaFil: Cascone, Osvaldo. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Microbiología, Inmunología y Biotecnología. Cátedra de Microbiología Industrial y Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Santos, Nuno C.. Universidade Nova de Lisboa. Faculdade de Ciencias Medicas.; PortugalFil: Disalvo, Edgardo Anibal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; ArgentinaFil: Hollmann, Axel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnologia. Instituto de Microbiologia Basica y Aplicada.; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina. Universidade Nova de Lisboa. Faculdade de Ciencias Medicas.; PortugalElsevier Science2014-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/105284Bouchet, Ana María; Iannucci, Nancy Beatriz; Pastrian, María Belén; Cascone, Osvaldo; Santos, Nuno C.; et al.; Biological activity of antibacterial peptides matches synergism between electrostatic and non electrostatic forces; Elsevier Science; Colloids and Surfaces B: Biointerfaces; 114; 7-2014; 363-3710927-7765CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://authors.elsevier.com/sd/article/S0927776513006656.info:eu-repo/semantics/altIdentifier/doi/10.1016/j.colsurfb.2013.10.025info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:47:44Zoai:ri.conicet.gov.ar:11336/105284instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:47:44.73CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
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 María
ANTIMICROBIAL PEPTIDE
LYSOZYME
PEPTIDEMEMBRANE INTERACTION
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
dc.creator.none.fl_str_mv Bouchet, Ana María
Iannucci, Nancy Beatriz
Pastrian, María Belén
Cascone, Osvaldo
Santos, Nuno C.
Disalvo, Edgardo Anibal
Hollmann, Axel
author Bouchet, Ana María
author_facet Bouchet, Ana María
Iannucci, Nancy Beatriz
Pastrian, María Belén
Cascone, Osvaldo
Santos, Nuno C.
Disalvo, Edgardo Anibal
Hollmann, Axel
author_role author
author2 Iannucci, Nancy Beatriz
Pastrian, María Belén
Cascone, Osvaldo
Santos, Nuno C.
Disalvo, Edgardo Anibal
Hollmann, Axel
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv ANTIMICROBIAL PEPTIDE
LYSOZYME
PEPTIDEMEMBRANE INTERACTION
HYDROPHILIC HYDROPHOBIC SYNERGISM
topic ANTIMICROBIAL PEPTIDE
LYSOZYME
PEPTIDEMEMBRANE INTERACTION
HYDROPHILIC HYDROPHOBIC SYNERGISM
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.4
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv 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 very high concentrations. This analog displays an additional positive charge near the N-terminus (108) and an extra Trp residue at the center of the molecule (111), indicating that this particular amino acid sequence improves its interaction with the bacterial plasma membrane. In order to understand the role of this arrangement 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 liposomes and lipid monolayers were evaluated by monitoring the changes in the fluorescence of the Trp residues and the variation of the monolayers surface pressure, respectively. Results obtained with both techniques revealed a significant affinity increase of [K108W111]107–115 hLz for lipids, especially when the membranes containing negatively charged lipids, such as phosphatidylglycerol. However,there is also a significant interaction with zwitterionic lipids, suggesting that other forces in addition to electrostatic interactions are involved in the binding. The analysis of adsorption isotherms and the insertion kinetics suggest that relaxation processes of the membrane structure are involved in the insertion process of novel peptide [K108W111]107–115 hLz but not in 107–115 hLz, probably by imposing a reorganization of water at the interphases. In this regard, the enhanced activity of peptide [K108W111]107–115 hLz may be explained by a synergistic effect between the increased electrostatic forces as well as the increased hydrophobic interactions.
Fil: Bouchet, Ana María. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
Fil: Iannucci, Nancy Beatriz. Romikin S.a; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Microbiología, Inmunología y Biotecnología. Cátedra de Microbiología Industrial y Biotecnología; Argentina
Fil: Pastrian, María Belén. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Microbiología, Inmunología y Biotecnología. Cátedra de Microbiología Industrial y Biotecnología; Argentina
Fil: Cascone, Osvaldo. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Microbiología, Inmunología y Biotecnología. Cátedra de Microbiología Industrial y Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Santos, Nuno C.. Universidade Nova de Lisboa. Faculdade de Ciencias Medicas.; Portugal
Fil: Disalvo, Edgardo Anibal. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
Fil: Hollmann, Axel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnologia. Instituto de Microbiologia Basica y Aplicada.; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina. Universidade Nova de Lisboa. Faculdade de Ciencias Medicas.; Portugal
description 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 very high concentrations. This analog displays an additional positive charge near the N-terminus (108) and an extra Trp residue at the center of the molecule (111), indicating that this particular amino acid sequence improves its interaction with the bacterial plasma membrane. In order to understand the role of this arrangement 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 liposomes and lipid monolayers were evaluated by monitoring the changes in the fluorescence of the Trp residues and the variation of the monolayers surface pressure, respectively. Results obtained with both techniques revealed a significant affinity increase of [K108W111]107–115 hLz for lipids, especially when the membranes containing negatively charged lipids, such as phosphatidylglycerol. However,there is also a significant interaction with zwitterionic lipids, suggesting that other forces in addition to electrostatic interactions are involved in the binding. The analysis of adsorption isotherms and the insertion kinetics suggest that relaxation processes of the membrane structure are involved in the insertion process of novel peptide [K108W111]107–115 hLz but not in 107–115 hLz, probably by imposing a reorganization of water at the interphases. In this regard, the enhanced activity of peptide [K108W111]107–115 hLz may be explained by a synergistic effect between the increased electrostatic forces as well as the increased hydrophobic interactions.
publishDate 2014
dc.date.none.fl_str_mv 2014-07
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/105284
Bouchet, Ana María; Iannucci, Nancy Beatriz; Pastrian, María Belén; Cascone, Osvaldo; Santos, Nuno C.; et al.; Biological activity of antibacterial peptides matches synergism between electrostatic and non electrostatic forces; Elsevier Science; Colloids and Surfaces B: Biointerfaces; 114; 7-2014; 363-371
0927-7765
CONICET Digital
CONICET
url http://hdl.handle.net/11336/105284
identifier_str_mv Bouchet, Ana María; Iannucci, Nancy Beatriz; Pastrian, María Belén; Cascone, Osvaldo; Santos, Nuno C.; et al.; Biological activity of antibacterial peptides matches synergism between electrostatic and non electrostatic forces; Elsevier Science; Colloids and Surfaces B: Biointerfaces; 114; 7-2014; 363-371
0927-7765
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://authors.elsevier.com/sd/article/S0927776513006656.
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.colsurfb.2013.10.025
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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