Effect of Anionic Antimicrobial Peptides on model lipid membranes

Autores
Noe, Melania Macarena; Rodríguez, Jésica Ayelén; Barredo, Gabriela Romina; Camperi, Silvia Andrea; Perillo, Maria Angelica; Nolan, María Verónica
Año de publicación
2023
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
Anionic antimicrobial peptides (AAPs) were first described in the early 1980s. They have been identified as part of the innate immune system of vertebrates, invertebrates and plants and are active against bacteria, fungi, viruses and pests such as insects. Membrane interaction appears to be key to the antimicrobial function of AAMPs. In the present work, we use the anionic peptide β-lg125-135, obtained from the tryptic hydrolysate of β- lactoglobulin, and evaluate its interaction with model membranes. We use DPPC or DPPC:DPPG mixtures as models of eukaryotic and bacterial membranes, respectively. In previous work we have shown that β-lg125-135 interacts preferentially with anionic monolayers. In the present work we investigate the effect of β-lg125-135 on membrane order and permeability. Unilamellar vesicles were used as model membranes. DPH and TMA-DPH fluorescence anisotropy were used to evaluate the effect of peptide interaction on membrane order: The DPH probe detects the hydrocarbon region, whereas the fluorescent probe TMA-DPH, with an additional charged group, is anchored at the lipid/ water interface and reports on a bilayer region distinct from that of the hydrophobic DPH, which detects a deeper region. The results obtained show that for vesicles composed of the equimolar lipid mixture, the anisotropy of both probes tested increases in the presence of peptide. For dpPC vesicles, this effect was less pronounced at the temperatures tested. This would indicate that the peptide partitions into the lipid mixing bilayers, increasing the molecular order. The effect of peptide-membrane interaction on vesicle permeability was assessed as the release of carboxyfluorescein entrapped in liposomes. We measured the increase in carboxyfluorescein fluorescence intensity with increasing AAP concentrations to elucidate the relationship between bilayer disruption and lipid bilayer perturbation. The results obtained showed that the higher the peptidelipid molar ratio, the higher the percentage of release of the fluorescent probe.
Fil: Noe, Melania Macarena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina
Fil: Rodríguez, Jésica Ayelén. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina
Fil: Barredo, Gabriela Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina
Fil: Camperi, Silvia Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina
Fil: Perillo, Maria Angelica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina
Fil: Nolan, María Verónica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina
LI Reunión Anual de la Sociedad Argentina de Biofísica
Córdoba
Argentina
Sociedad Argentina de Biofísica
Materia
ANIONIC PEPTIDES
ANTIMICROBIAL PEPTIDES
MONOLAYERS
LIPID-PEPTIDE INTERACTION
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:11336/257200
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/257200
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Effect of Anionic Antimicrobial Peptides on model lipid membranesNoe, Melania MacarenaRodríguez, Jésica AyelénBarredo, Gabriela RominaCamperi, Silvia AndreaPerillo, Maria AngelicaNolan, María VerónicaANIONIC PEPTIDESANTIMICROBIAL PEPTIDESMONOLAYERSLIPID-PEPTIDE INTERACTIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Anionic antimicrobial peptides (AAPs) were first described in the early 1980s. They have been identified as part of the innate immune system of vertebrates, invertebrates and plants and are active against bacteria, fungi, viruses and pests such as insects. Membrane interaction appears to be key to the antimicrobial function of AAMPs. In the present work, we use the anionic peptide β-lg125-135, obtained from the tryptic hydrolysate of β- lactoglobulin, and evaluate its interaction with model membranes. We use DPPC or DPPC:DPPG mixtures as models of eukaryotic and bacterial membranes, respectively. In previous work we have shown that β-lg125-135 interacts preferentially with anionic monolayers. In the present work we investigate the effect of β-lg125-135 on membrane order and permeability. Unilamellar vesicles were used as model membranes. DPH and TMA-DPH fluorescence anisotropy were used to evaluate the effect of peptide interaction on membrane order: The DPH probe detects the hydrocarbon region, whereas the fluorescent probe TMA-DPH, with an additional charged group, is anchored at the lipid/ water interface and reports on a bilayer region distinct from that of the hydrophobic DPH, which detects a deeper region. The results obtained show that for vesicles composed of the equimolar lipid mixture, the anisotropy of both probes tested increases in the presence of peptide. For dpPC vesicles, this effect was less pronounced at the temperatures tested. This would indicate that the peptide partitions into the lipid mixing bilayers, increasing the molecular order. The effect of peptide-membrane interaction on vesicle permeability was assessed as the release of carboxyfluorescein entrapped in liposomes. We measured the increase in carboxyfluorescein fluorescence intensity with increasing AAP concentrations to elucidate the relationship between bilayer disruption and lipid bilayer perturbation. The results obtained showed that the higher the peptidelipid molar ratio, the higher the percentage of release of the fluorescent probe.Fil: Noe, Melania Macarena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; ArgentinaFil: Rodríguez, Jésica Ayelén. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; ArgentinaFil: Barredo, Gabriela Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; ArgentinaFil: Camperi, Silvia Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; ArgentinaFil: Perillo, Maria Angelica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; ArgentinaFil: Nolan, María Verónica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; ArgentinaLI Reunión Anual de la Sociedad Argentina de BiofísicaCórdobaArgentinaSociedad Argentina de BiofísicaSociedad Argentina de BiofísicaAcierno, Juan PabloCelej, Maria SoledadVazquez, Diego Sebastian2023info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectReuniónBookhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/vnd.openxmlformats-officedocument.wordprocessingml.documentapplication/pdfhttp://hdl.handle.net/11336/257200Effect of Anionic Antimicrobial Peptides on model lipid membranes; LI Reunión Anual de la Sociedad Argentina de Biofísica; Córdoba; Argentina; 2023; 147-147978-987-48938-1-9CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://biofisica.org.ar/congreso-2023/Nacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:30:05Zoai:ri.conicet.gov.ar:11336/257200instacron: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 11:30:05.524CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Effect of Anionic Antimicrobial Peptides on model lipid membranes
title Effect of Anionic Antimicrobial Peptides on model lipid membranes
spellingShingle Effect of Anionic Antimicrobial Peptides on model lipid membranes
Noe, Melania Macarena
ANIONIC PEPTIDES
ANTIMICROBIAL PEPTIDES
MONOLAYERS
LIPID-PEPTIDE INTERACTION
title_short Effect of Anionic Antimicrobial Peptides on model lipid membranes
title_full Effect of Anionic Antimicrobial Peptides on model lipid membranes
title_fullStr Effect of Anionic Antimicrobial Peptides on model lipid membranes
title_full_unstemmed Effect of Anionic Antimicrobial Peptides on model lipid membranes
title_sort Effect of Anionic Antimicrobial Peptides on model lipid membranes
dc.creator.none.fl_str_mv Noe, Melania Macarena
Rodríguez, Jésica Ayelén
Barredo, Gabriela Romina
Camperi, Silvia Andrea
Perillo, Maria Angelica
Nolan, María Verónica
author Noe, Melania Macarena
author_facet Noe, Melania Macarena
Rodríguez, Jésica Ayelén
Barredo, Gabriela Romina
Camperi, Silvia Andrea
Perillo, Maria Angelica
Nolan, María Verónica
author_role author
author2 Rodríguez, Jésica Ayelén
Barredo, Gabriela Romina
Camperi, Silvia Andrea
Perillo, Maria Angelica
Nolan, María Verónica
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Acierno, Juan Pablo
Celej, Maria Soledad
Vazquez, Diego Sebastian
dc.subject.none.fl_str_mv ANIONIC PEPTIDES
ANTIMICROBIAL PEPTIDES
MONOLAYERS
LIPID-PEPTIDE INTERACTION
topic ANIONIC PEPTIDES
ANTIMICROBIAL PEPTIDES
MONOLAYERS
LIPID-PEPTIDE INTERACTION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Anionic antimicrobial peptides (AAPs) were first described in the early 1980s. They have been identified as part of the innate immune system of vertebrates, invertebrates and plants and are active against bacteria, fungi, viruses and pests such as insects. Membrane interaction appears to be key to the antimicrobial function of AAMPs. In the present work, we use the anionic peptide β-lg125-135, obtained from the tryptic hydrolysate of β- lactoglobulin, and evaluate its interaction with model membranes. We use DPPC or DPPC:DPPG mixtures as models of eukaryotic and bacterial membranes, respectively. In previous work we have shown that β-lg125-135 interacts preferentially with anionic monolayers. In the present work we investigate the effect of β-lg125-135 on membrane order and permeability. Unilamellar vesicles were used as model membranes. DPH and TMA-DPH fluorescence anisotropy were used to evaluate the effect of peptide interaction on membrane order: The DPH probe detects the hydrocarbon region, whereas the fluorescent probe TMA-DPH, with an additional charged group, is anchored at the lipid/ water interface and reports on a bilayer region distinct from that of the hydrophobic DPH, which detects a deeper region. The results obtained show that for vesicles composed of the equimolar lipid mixture, the anisotropy of both probes tested increases in the presence of peptide. For dpPC vesicles, this effect was less pronounced at the temperatures tested. This would indicate that the peptide partitions into the lipid mixing bilayers, increasing the molecular order. The effect of peptide-membrane interaction on vesicle permeability was assessed as the release of carboxyfluorescein entrapped in liposomes. We measured the increase in carboxyfluorescein fluorescence intensity with increasing AAP concentrations to elucidate the relationship between bilayer disruption and lipid bilayer perturbation. The results obtained showed that the higher the peptidelipid molar ratio, the higher the percentage of release of the fluorescent probe.
Fil: Noe, Melania Macarena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina
Fil: Rodríguez, Jésica Ayelén. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina
Fil: Barredo, Gabriela Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina
Fil: Camperi, Silvia Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina
Fil: Perillo, Maria Angelica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina
Fil: Nolan, María Verónica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina
LI Reunión Anual de la Sociedad Argentina de Biofísica
Córdoba
Argentina
Sociedad Argentina de Biofísica
description Anionic antimicrobial peptides (AAPs) were first described in the early 1980s. They have been identified as part of the innate immune system of vertebrates, invertebrates and plants and are active against bacteria, fungi, viruses and pests such as insects. Membrane interaction appears to be key to the antimicrobial function of AAMPs. In the present work, we use the anionic peptide β-lg125-135, obtained from the tryptic hydrolysate of β- lactoglobulin, and evaluate its interaction with model membranes. We use DPPC or DPPC:DPPG mixtures as models of eukaryotic and bacterial membranes, respectively. In previous work we have shown that β-lg125-135 interacts preferentially with anionic monolayers. In the present work we investigate the effect of β-lg125-135 on membrane order and permeability. Unilamellar vesicles were used as model membranes. DPH and TMA-DPH fluorescence anisotropy were used to evaluate the effect of peptide interaction on membrane order: The DPH probe detects the hydrocarbon region, whereas the fluorescent probe TMA-DPH, with an additional charged group, is anchored at the lipid/ water interface and reports on a bilayer region distinct from that of the hydrophobic DPH, which detects a deeper region. The results obtained show that for vesicles composed of the equimolar lipid mixture, the anisotropy of both probes tested increases in the presence of peptide. For dpPC vesicles, this effect was less pronounced at the temperatures tested. This would indicate that the peptide partitions into the lipid mixing bilayers, increasing the molecular order. The effect of peptide-membrane interaction on vesicle permeability was assessed as the release of carboxyfluorescein entrapped in liposomes. We measured the increase in carboxyfluorescein fluorescence intensity with increasing AAP concentrations to elucidate the relationship between bilayer disruption and lipid bilayer perturbation. The results obtained showed that the higher the peptidelipid molar ratio, the higher the percentage of release of the fluorescent probe.
publishDate 2023
dc.date.none.fl_str_mv 2023
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/conferenceObject
Reunión
Book
http://purl.org/coar/resource_type/c_5794
info:ar-repo/semantics/documentoDeConferencia
status_str publishedVersion
format conferenceObject
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/257200
Effect of Anionic Antimicrobial Peptides on model lipid membranes; LI Reunión Anual de la Sociedad Argentina de Biofísica; Córdoba; Argentina; 2023; 147-147
978-987-48938-1-9
CONICET Digital
CONICET
url http://hdl.handle.net/11336/257200
identifier_str_mv Effect of Anionic Antimicrobial Peptides on model lipid membranes; LI Reunión Anual de la Sociedad Argentina de Biofísica; Córdoba; Argentina; 2023; 147-147
978-987-48938-1-9
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://biofisica.org.ar/congreso-2023/
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/vnd.openxmlformats-officedocument.wordprocessingml.document
application/pdf
dc.coverage.none.fl_str_mv Nacional
dc.publisher.none.fl_str_mv Sociedad Argentina de Biofísica
publisher.none.fl_str_mv Sociedad Argentina de Biofísica
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
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