Antifungal Peptides SmAPα1–21 and SmAPγ27–44 Designed from Different Loops of DefSm2-D Have Distinct Modes of Action

Autores
Iturralde, Micaela; Bracho, Juan Pablo; Valdivia Pérez, Jessica Aye; Guzmán, Fanny; Malbrán, Ismael; Maté, Sabina María; Fanani, Maria Laura; Vairo Cavalli, Sandra Elizabeth
Año de publicación
2025
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Background: The use of antimicrobial peptides (AMPs) as biotechnological tools is an area of growing interest in the research that seeks to improve crop defense. SmAPα1–21 and SmAPγ27–44 were previously reported to inhibit Fusarium graminearum, permeabilize the plasma membrane and induce cytoplasmic disorganization. To exert its activity, SmAPα1–21 initially enters through the basal and apical cells of F. graminearum conidia and then displays a general but non-homogeneous distribution in the cytoplasm of all conidial cells, in contrast. Methods: We analyzed, focusing on membrane interaction, the mode of action of SmAPγ27–44, a peptide based on the γ-core of defensins DefSm2-D and DefSm3, and SmAPα1–21, based on the α-core of DefSm2-D. Additionally, we compared the behavior of SmAPα1–21 with that of SmAP3α1–21 based on DefSm3 but with no activity against F. graminearum. Results: In this study, we showed that SmAPγ27–44 enters the cells with discrete intracellular localization. Furthermore, both peptides disrupted the plasma membrane, but with different modes of action. When large unilamellar liposomes (LUVs) containing phosphatidic acid and ergosterol were used as a filamentous fungal plasma membrane model, SmAPγ27–44 strongly induced aggregation concomitantly with the solubilization of the liposomes and showed the maximal insertion of its tryptophan moiety into the membrane’s hydrophobic interior. In comparison, SmAPα1–21 showed a high effect on the ζ potential of anionic vesicles, vesicle aggregation capacity after reaching a concentration threshold, and moderate transfer of tryptophan to the membrane. SmAP3α1–21, on the other hand, showed poor superficial adsorption to liposomes. Conclusions: In view of our results, a cell penetration peptide-like effect was pictured for the γ-core defensin-derived peptide and a classical AMP action was observed for the α-core defensin-derived one.
Fil: Iturralde, Micaela. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Fil: Bracho, Juan Pablo. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Valdivia Pérez, Jessica Aye. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Guzmán, Fanny. Pontificia Universidad Católica de Valparaíso; Chile
Fil: Malbrán, Ismael. Universidad Nacional de La Plata. Facultad de Ciencias Agrarias y Forestales. Departamento de Ciencias Biológicas. Centro de Investigaciones de Fitopatología. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigaciones de Fitopatología; Argentina
Fil: Maté, Sabina María. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
Fil: Fanani, Maria Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Vairo Cavalli, Sandra Elizabeth. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Materia
ANTIFUNGAL PEPTIDES
DEFENSIN-DERIVED PEPTIDES
SILYBUM MARIANUM
FUSARIUM GRAMINEARUM
PEPTIDE–MEMBRANE INTERACTION
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/267057
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Antifungal Peptides SmAPα1–21 and SmAPγ27–44 Designed from Different Loops of DefSm2-D Have Distinct Modes of ActionIturralde, MicaelaBracho, Juan PabloValdivia Pérez, Jessica AyeGuzmán, FannyMalbrán, IsmaelMaté, Sabina MaríaFanani, Maria LauraVairo Cavalli, Sandra ElizabethANTIFUNGAL PEPTIDESDEFENSIN-DERIVED PEPTIDESSILYBUM MARIANUMFUSARIUM GRAMINEARUMPEPTIDE–MEMBRANE INTERACTIONhttps://purl.org/becyt/ford/4.1https://purl.org/becyt/ford/4https://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Background: The use of antimicrobial peptides (AMPs) as biotechnological tools is an area of growing interest in the research that seeks to improve crop defense. SmAPα1–21 and SmAPγ27–44 were previously reported to inhibit Fusarium graminearum, permeabilize the plasma membrane and induce cytoplasmic disorganization. To exert its activity, SmAPα1–21 initially enters through the basal and apical cells of F. graminearum conidia and then displays a general but non-homogeneous distribution in the cytoplasm of all conidial cells, in contrast. Methods: We analyzed, focusing on membrane interaction, the mode of action of SmAPγ27–44, a peptide based on the γ-core of defensins DefSm2-D and DefSm3, and SmAPα1–21, based on the α-core of DefSm2-D. Additionally, we compared the behavior of SmAPα1–21 with that of SmAP3α1–21 based on DefSm3 but with no activity against F. graminearum. Results: In this study, we showed that SmAPγ27–44 enters the cells with discrete intracellular localization. Furthermore, both peptides disrupted the plasma membrane, but with different modes of action. When large unilamellar liposomes (LUVs) containing phosphatidic acid and ergosterol were used as a filamentous fungal plasma membrane model, SmAPγ27–44 strongly induced aggregation concomitantly with the solubilization of the liposomes and showed the maximal insertion of its tryptophan moiety into the membrane’s hydrophobic interior. In comparison, SmAPα1–21 showed a high effect on the ζ potential of anionic vesicles, vesicle aggregation capacity after reaching a concentration threshold, and moderate transfer of tryptophan to the membrane. SmAP3α1–21, on the other hand, showed poor superficial adsorption to liposomes. Conclusions: In view of our results, a cell penetration peptide-like effect was pictured for the γ-core defensin-derived peptide and a classical AMP action was observed for the α-core defensin-derived one.Fil: Iturralde, Micaela. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; ArgentinaFil: Bracho, Juan Pablo. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; ArgentinaFil: Valdivia Pérez, Jessica Aye. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Guzmán, Fanny. Pontificia Universidad Católica de Valparaíso; ChileFil: Malbrán, Ismael. Universidad Nacional de La Plata. Facultad de Ciencias Agrarias y Forestales. Departamento de Ciencias Biológicas. Centro de Investigaciones de Fitopatología. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigaciones de Fitopatología; ArgentinaFil: Maté, Sabina María. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; ArgentinaFil: Fanani, Maria Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Vairo Cavalli, Sandra Elizabeth. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; ArgentinaMultidisciplinary Digital Publishing Institute2025-04info: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/11336/267057Iturralde, Micaela; Bracho, Juan Pablo; Valdivia Pérez, Jessica Aye; Guzmán, Fanny; Malbrán, Ismael; et al.; Antifungal Peptides SmAPα1–21 and SmAPγ27–44 Designed from Different Loops of DefSm2-D Have Distinct Modes of Action; Multidisciplinary Digital Publishing Institute; Antibiotics; 14; 5; 4-2025; 430-4512079-6382CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2079-6382/14/5/430info:eu-repo/semantics/altIdentifier/doi/10.3390/antibiotics14050430info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:51:11Zoai:ri.conicet.gov.ar:11336/267057instacron: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 09:51:11.864CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Antifungal Peptides SmAPα1–21 and SmAPγ27–44 Designed from Different Loops of DefSm2-D Have Distinct Modes of Action
title Antifungal Peptides SmAPα1–21 and SmAPγ27–44 Designed from Different Loops of DefSm2-D Have Distinct Modes of Action
spellingShingle Antifungal Peptides SmAPα1–21 and SmAPγ27–44 Designed from Different Loops of DefSm2-D Have Distinct Modes of Action
Iturralde, Micaela
ANTIFUNGAL PEPTIDES
DEFENSIN-DERIVED PEPTIDES
SILYBUM MARIANUM
FUSARIUM GRAMINEARUM
PEPTIDE–MEMBRANE INTERACTION
title_short Antifungal Peptides SmAPα1–21 and SmAPγ27–44 Designed from Different Loops of DefSm2-D Have Distinct Modes of Action
title_full Antifungal Peptides SmAPα1–21 and SmAPγ27–44 Designed from Different Loops of DefSm2-D Have Distinct Modes of Action
title_fullStr Antifungal Peptides SmAPα1–21 and SmAPγ27–44 Designed from Different Loops of DefSm2-D Have Distinct Modes of Action
title_full_unstemmed Antifungal Peptides SmAPα1–21 and SmAPγ27–44 Designed from Different Loops of DefSm2-D Have Distinct Modes of Action
title_sort Antifungal Peptides SmAPα1–21 and SmAPγ27–44 Designed from Different Loops of DefSm2-D Have Distinct Modes of Action
dc.creator.none.fl_str_mv Iturralde, Micaela
Bracho, Juan Pablo
Valdivia Pérez, Jessica Aye
Guzmán, Fanny
Malbrán, Ismael
Maté, Sabina María
Fanani, Maria Laura
Vairo Cavalli, Sandra Elizabeth
author Iturralde, Micaela
author_facet Iturralde, Micaela
Bracho, Juan Pablo
Valdivia Pérez, Jessica Aye
Guzmán, Fanny
Malbrán, Ismael
Maté, Sabina María
Fanani, Maria Laura
Vairo Cavalli, Sandra Elizabeth
author_role author
author2 Bracho, Juan Pablo
Valdivia Pérez, Jessica Aye
Guzmán, Fanny
Malbrán, Ismael
Maté, Sabina María
Fanani, Maria Laura
Vairo Cavalli, Sandra Elizabeth
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv ANTIFUNGAL PEPTIDES
DEFENSIN-DERIVED PEPTIDES
SILYBUM MARIANUM
FUSARIUM GRAMINEARUM
PEPTIDE–MEMBRANE INTERACTION
topic ANTIFUNGAL PEPTIDES
DEFENSIN-DERIVED PEPTIDES
SILYBUM MARIANUM
FUSARIUM GRAMINEARUM
PEPTIDE–MEMBRANE INTERACTION
purl_subject.fl_str_mv https://purl.org/becyt/ford/4.1
https://purl.org/becyt/ford/4
https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Background: The use of antimicrobial peptides (AMPs) as biotechnological tools is an area of growing interest in the research that seeks to improve crop defense. SmAPα1–21 and SmAPγ27–44 were previously reported to inhibit Fusarium graminearum, permeabilize the plasma membrane and induce cytoplasmic disorganization. To exert its activity, SmAPα1–21 initially enters through the basal and apical cells of F. graminearum conidia and then displays a general but non-homogeneous distribution in the cytoplasm of all conidial cells, in contrast. Methods: We analyzed, focusing on membrane interaction, the mode of action of SmAPγ27–44, a peptide based on the γ-core of defensins DefSm2-D and DefSm3, and SmAPα1–21, based on the α-core of DefSm2-D. Additionally, we compared the behavior of SmAPα1–21 with that of SmAP3α1–21 based on DefSm3 but with no activity against F. graminearum. Results: In this study, we showed that SmAPγ27–44 enters the cells with discrete intracellular localization. Furthermore, both peptides disrupted the plasma membrane, but with different modes of action. When large unilamellar liposomes (LUVs) containing phosphatidic acid and ergosterol were used as a filamentous fungal plasma membrane model, SmAPγ27–44 strongly induced aggregation concomitantly with the solubilization of the liposomes and showed the maximal insertion of its tryptophan moiety into the membrane’s hydrophobic interior. In comparison, SmAPα1–21 showed a high effect on the ζ potential of anionic vesicles, vesicle aggregation capacity after reaching a concentration threshold, and moderate transfer of tryptophan to the membrane. SmAP3α1–21, on the other hand, showed poor superficial adsorption to liposomes. Conclusions: In view of our results, a cell penetration peptide-like effect was pictured for the γ-core defensin-derived peptide and a classical AMP action was observed for the α-core defensin-derived one.
Fil: Iturralde, Micaela. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Fil: Bracho, Juan Pablo. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Valdivia Pérez, Jessica Aye. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Guzmán, Fanny. Pontificia Universidad Católica de Valparaíso; Chile
Fil: Malbrán, Ismael. Universidad Nacional de La Plata. Facultad de Ciencias Agrarias y Forestales. Departamento de Ciencias Biológicas. Centro de Investigaciones de Fitopatología. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigaciones de Fitopatología; Argentina
Fil: Maté, Sabina María. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
Fil: Fanani, Maria Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Vairo Cavalli, Sandra Elizabeth. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
description Background: The use of antimicrobial peptides (AMPs) as biotechnological tools is an area of growing interest in the research that seeks to improve crop defense. SmAPα1–21 and SmAPγ27–44 were previously reported to inhibit Fusarium graminearum, permeabilize the plasma membrane and induce cytoplasmic disorganization. To exert its activity, SmAPα1–21 initially enters through the basal and apical cells of F. graminearum conidia and then displays a general but non-homogeneous distribution in the cytoplasm of all conidial cells, in contrast. Methods: We analyzed, focusing on membrane interaction, the mode of action of SmAPγ27–44, a peptide based on the γ-core of defensins DefSm2-D and DefSm3, and SmAPα1–21, based on the α-core of DefSm2-D. Additionally, we compared the behavior of SmAPα1–21 with that of SmAP3α1–21 based on DefSm3 but with no activity against F. graminearum. Results: In this study, we showed that SmAPγ27–44 enters the cells with discrete intracellular localization. Furthermore, both peptides disrupted the plasma membrane, but with different modes of action. When large unilamellar liposomes (LUVs) containing phosphatidic acid and ergosterol were used as a filamentous fungal plasma membrane model, SmAPγ27–44 strongly induced aggregation concomitantly with the solubilization of the liposomes and showed the maximal insertion of its tryptophan moiety into the membrane’s hydrophobic interior. In comparison, SmAPα1–21 showed a high effect on the ζ potential of anionic vesicles, vesicle aggregation capacity after reaching a concentration threshold, and moderate transfer of tryptophan to the membrane. SmAP3α1–21, on the other hand, showed poor superficial adsorption to liposomes. Conclusions: In view of our results, a cell penetration peptide-like effect was pictured for the γ-core defensin-derived peptide and a classical AMP action was observed for the α-core defensin-derived one.
publishDate 2025
dc.date.none.fl_str_mv 2025-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
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info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/267057
Iturralde, Micaela; Bracho, Juan Pablo; Valdivia Pérez, Jessica Aye; Guzmán, Fanny; Malbrán, Ismael; et al.; Antifungal Peptides SmAPα1–21 and SmAPγ27–44 Designed from Different Loops of DefSm2-D Have Distinct Modes of Action; Multidisciplinary Digital Publishing Institute; Antibiotics; 14; 5; 4-2025; 430-451
2079-6382
CONICET Digital
CONICET
url http://hdl.handle.net/11336/267057
identifier_str_mv Iturralde, Micaela; Bracho, Juan Pablo; Valdivia Pérez, Jessica Aye; Guzmán, Fanny; Malbrán, Ismael; et al.; Antifungal Peptides SmAPα1–21 and SmAPγ27–44 Designed from Different Loops of DefSm2-D Have Distinct Modes of Action; Multidisciplinary Digital Publishing Institute; Antibiotics; 14; 5; 4-2025; 430-451
2079-6382
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://www.mdpi.com/2079-6382/14/5/430
info:eu-repo/semantics/altIdentifier/doi/10.3390/antibiotics14050430
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eu_rights_str_mv openAccess
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application/pdf
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application/pdf
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dc.publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
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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