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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/257200
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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 Técnicas2025-09-29T10:00:36Zoai: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:34982025-09-29 10:00:36.379CONICET 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 |
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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 |
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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 |
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eng |
language |
eng |
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Sociedad Argentina de Biofísica |
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Sociedad Argentina de Biofísica |
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