The dynamic action mechanism of small cationic antimicrobial peptides

Autores
Lopez Cascales, J. J.; Garro, Adriana; Porasso, Rodolfo Daniel; Enriz, Ricardo Daniel
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Antimicrobial peptides form part of the immune system as protection against the action of external pathogens. The differences that exist between mammalian and microbial cell membrane architectures
are key aspects of the ability of these peptides to discriminate between pathogens and host cells. Given that the pathogen membrane is the non-specific target of these cationic peptides, different molecular
mechanisms have been suggested to describe the rules that permit them to distinguish between pathogens and mammalian cells. In this context, and setting aside the old fashion idea that cationic peptides act through one mechanism alone, this work will provide insight into the molecular action mechanism of small antimicrobial peptides, based on molecular dynamics simulations of phospholipid bilayers that mimic different cell membrane architectures. After measuring different properties of these
lipid bilayers, in the absence and presence of peptides, a four-step action mechanism was suggested on the basis of the formation of phospholipid rafts induced by the presence of these cationic peptides. Thus, this work shows how differences in the bending modulus (k b ) of these lipid rafts and differences in the free energy profiles (DG(z)) associated with the insertion of these peptides into these lipid rafts are key aspects for explaining the action mechanism of these cationic peptides at the molecular level.
Fil: Lopez Cascales, J. J.. Universidad Politecnica de Cartagena; España
Fil: Garro, Adriana. Universidad Politecnica de Cartagena; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
Fil: Porasso, Rodolfo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto de Matemática Aplicada de San Luis; Argentina
Fil: Enriz, Ricardo Daniel. Universidad Politecnica de Cartagena; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
Materia
Cationic Peptides
Membranes
Molecular Dynamics
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:11336/5808
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/5808
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The dynamic action mechanism of small cationic antimicrobial peptidesLopez Cascales, J. J.Garro, AdrianaPorasso, Rodolfo DanielEnriz, Ricardo DanielCationic PeptidesMembranesMolecular Dynamicshttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Antimicrobial peptides form part of the immune system as protection against the action of external pathogens. The differences that exist between mammalian and microbial cell membrane architectures<br />are key aspects of the ability of these peptides to discriminate between pathogens and host cells. Given that the pathogen membrane is the non-specific target of these cationic peptides, different molecular<br />mechanisms have been suggested to describe the rules that permit them to distinguish between pathogens and mammalian cells. In this context, and setting aside the old fashion idea that cationic peptides act through one mechanism alone, this work will provide insight into the molecular action mechanism of small antimicrobial peptides, based on molecular dynamics simulations of phospholipid bilayers that mimic different cell membrane architectures. After measuring different properties of these<br />lipid bilayers, in the absence and presence of peptides, a four-step action mechanism was suggested on the basis of the formation of phospholipid rafts induced by the presence of these cationic peptides. Thus, this work shows how differences in the bending modulus (k b ) of these lipid rafts and differences in the free energy profiles (DG(z)) associated with the insertion of these peptides into these lipid rafts are key aspects for explaining the action mechanism of these cationic peptides at the molecular level.Fil: Lopez Cascales, J. J.. Universidad Politecnica de Cartagena; EspañaFil: Garro, Adriana. Universidad Politecnica de Cartagena; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; ArgentinaFil: Porasso, Rodolfo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto de Matemática Aplicada de San Luis; ArgentinaFil: Enriz, Ricardo Daniel. Universidad Politecnica de Cartagena; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; ArgentinaRoyal Society Of Chemistry2014-09info: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/11336/5808Lopez Cascales, J. J.; Garro, Adriana; Porasso, Rodolfo Daniel; Enriz, Ricardo Daniel; The dynamic action mechanism of small cationic antimicrobial peptides; Royal Society Of Chemistry; Physical Chemistry Chemical Physics; 16; 39; 9-2014; 21694-217051463-9076enginfo:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/en/Content/ArticleLanding/2014/CP/c4cp02537ginfo:eu-repo/semantics/altIdentifier/doi/10.1039/C4CP02537Ginfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:17:10Zoai:ri.conicet.gov.ar:11336/5808instacron: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:34982025-10-22 11:17:10.54CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The dynamic action mechanism of small cationic antimicrobial peptides
title The dynamic action mechanism of small cationic antimicrobial peptides
spellingShingle The dynamic action mechanism of small cationic antimicrobial peptides
Lopez Cascales, J. J.
Cationic Peptides
Membranes
Molecular Dynamics
title_short The dynamic action mechanism of small cationic antimicrobial peptides
title_full The dynamic action mechanism of small cationic antimicrobial peptides
title_fullStr The dynamic action mechanism of small cationic antimicrobial peptides
title_full_unstemmed The dynamic action mechanism of small cationic antimicrobial peptides
title_sort The dynamic action mechanism of small cationic antimicrobial peptides
dc.creator.none.fl_str_mv Lopez Cascales, J. J.
Garro, Adriana
Porasso, Rodolfo Daniel
Enriz, Ricardo Daniel
author Lopez Cascales, J. J.
author_facet Lopez Cascales, J. J.
Garro, Adriana
Porasso, Rodolfo Daniel
Enriz, Ricardo Daniel
author_role author
author2 Garro, Adriana
Porasso, Rodolfo Daniel
Enriz, Ricardo Daniel
author2_role author
author
author
dc.subject.none.fl_str_mv Cationic Peptides
Membranes
Molecular Dynamics
topic Cationic Peptides
Membranes
Molecular Dynamics
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Antimicrobial peptides form part of the immune system as protection against the action of external pathogens. The differences that exist between mammalian and microbial cell membrane architectures<br />are key aspects of the ability of these peptides to discriminate between pathogens and host cells. Given that the pathogen membrane is the non-specific target of these cationic peptides, different molecular<br />mechanisms have been suggested to describe the rules that permit them to distinguish between pathogens and mammalian cells. In this context, and setting aside the old fashion idea that cationic peptides act through one mechanism alone, this work will provide insight into the molecular action mechanism of small antimicrobial peptides, based on molecular dynamics simulations of phospholipid bilayers that mimic different cell membrane architectures. After measuring different properties of these<br />lipid bilayers, in the absence and presence of peptides, a four-step action mechanism was suggested on the basis of the formation of phospholipid rafts induced by the presence of these cationic peptides. Thus, this work shows how differences in the bending modulus (k b ) of these lipid rafts and differences in the free energy profiles (DG(z)) associated with the insertion of these peptides into these lipid rafts are key aspects for explaining the action mechanism of these cationic peptides at the molecular level.
Fil: Lopez Cascales, J. J.. Universidad Politecnica de Cartagena; España
Fil: Garro, Adriana. Universidad Politecnica de Cartagena; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
Fil: Porasso, Rodolfo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto de Matemática Aplicada de San Luis; Argentina
Fil: Enriz, Ricardo Daniel. Universidad Politecnica de Cartagena; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
description Antimicrobial peptides form part of the immune system as protection against the action of external pathogens. The differences that exist between mammalian and microbial cell membrane architectures<br />are key aspects of the ability of these peptides to discriminate between pathogens and host cells. Given that the pathogen membrane is the non-specific target of these cationic peptides, different molecular<br />mechanisms have been suggested to describe the rules that permit them to distinguish between pathogens and mammalian cells. In this context, and setting aside the old fashion idea that cationic peptides act through one mechanism alone, this work will provide insight into the molecular action mechanism of small antimicrobial peptides, based on molecular dynamics simulations of phospholipid bilayers that mimic different cell membrane architectures. After measuring different properties of these<br />lipid bilayers, in the absence and presence of peptides, a four-step action mechanism was suggested on the basis of the formation of phospholipid rafts induced by the presence of these cationic peptides. Thus, this work shows how differences in the bending modulus (k b ) of these lipid rafts and differences in the free energy profiles (DG(z)) associated with the insertion of these peptides into these lipid rafts are key aspects for explaining the action mechanism of these cationic peptides at the molecular level.
publishDate 2014
dc.date.none.fl_str_mv 2014-09
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/11336/5808
Lopez Cascales, J. J.; Garro, Adriana; Porasso, Rodolfo Daniel; Enriz, Ricardo Daniel; The dynamic action mechanism of small cationic antimicrobial peptides; Royal Society Of Chemistry; Physical Chemistry Chemical Physics; 16; 39; 9-2014; 21694-21705
1463-9076
url http://hdl.handle.net/11336/5808
identifier_str_mv Lopez Cascales, J. J.; Garro, Adriana; Porasso, Rodolfo Daniel; Enriz, Ricardo Daniel; The dynamic action mechanism of small cationic antimicrobial peptides; Royal Society Of Chemistry; Physical Chemistry Chemical Physics; 16; 39; 9-2014; 21694-21705
1463-9076
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/en/Content/ArticleLanding/2014/CP/c4cp02537g
info:eu-repo/semantics/altIdentifier/doi/10.1039/C4CP02537G
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 Royal Society Of Chemistry
publisher.none.fl_str_mv Royal Society Of Chemistry
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 12.982451

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