Molecular view by Fourier transform infrared spectroscopy of the relationship between lactocin 705 and membranes: Speculations on antimicrobial mechanism
- Autores
- Castellano, Patricia Haydee; Vignolo, Graciela Margarita; Farias, Ricardo Norberto; Arrondo Jose Luis; Chehin, Rosana Nieves
- Año de publicación
- 2007
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Lactocin 705 is a bacteriocin whose activity depends upon the complementation of two peptides, termed Lac705α and Lac705β. Neither Lac705α nor Lac705β displayed bacteriocin activity by itself when the growth of sensitive cells was monitored. To obtain molecular insights into the lactocin 705 mechanism of action, Fourier transform infrared spectroscopy was used to investigate the interactions of each peptide (Lac705α and Lac705β) with dipalmitoylphosphatidylcholine liposomal membranes. Both peptides show the ability to interact with the zwitterionic membrane but at different bilayer levels. While Lac705α interacts with the interfacial region inducing dehydration, Lac705β peptide interacts with only the hydrophobic core. This paper presents the first experimental evidence that supports the hypothesis that Lac705α and Lac705β peptides could form a transmembrane oligomer. From the obtained results, a mechanism of action of lactocin 705 on membrane systems is proposed. The component Lac705α could induce the dehydration of the bilayer interfacial region, and the Lac705β peptide could insert in the hydrophobic region of the membrane where the peptide has adequate conditions to achieve the oligomerization.
Fil: Castellano, Patricia Haydee. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Vignolo, Graciela Margarita. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina
Fil: Farias, Ricardo Norberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Arrondo Jose Luis. Universidad Politécnica de Valencia; España
Fil: Chehin, Rosana Nieves. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina - Materia
-
Antimicrobial Peptide
Lactocin 705
Mechanism of Action
Ftir
Fourier Transform Infrared Spectroscopy - 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:11336/56340
Ver los metadatos del registro completo
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Molecular view by Fourier transform infrared spectroscopy of the relationship between lactocin 705 and membranes: Speculations on antimicrobial mechanismCastellano, Patricia HaydeeVignolo, Graciela MargaritaFarias, Ricardo NorbertoArrondo Jose LuisChehin, Rosana NievesAntimicrobial PeptideLactocin 705Mechanism of ActionFtirFourier Transform Infrared Spectroscopyhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Lactocin 705 is a bacteriocin whose activity depends upon the complementation of two peptides, termed Lac705α and Lac705β. Neither Lac705α nor Lac705β displayed bacteriocin activity by itself when the growth of sensitive cells was monitored. To obtain molecular insights into the lactocin 705 mechanism of action, Fourier transform infrared spectroscopy was used to investigate the interactions of each peptide (Lac705α and Lac705β) with dipalmitoylphosphatidylcholine liposomal membranes. Both peptides show the ability to interact with the zwitterionic membrane but at different bilayer levels. While Lac705α interacts with the interfacial region inducing dehydration, Lac705β peptide interacts with only the hydrophobic core. This paper presents the first experimental evidence that supports the hypothesis that Lac705α and Lac705β peptides could form a transmembrane oligomer. From the obtained results, a mechanism of action of lactocin 705 on membrane systems is proposed. The component Lac705α could induce the dehydration of the bilayer interfacial region, and the Lac705β peptide could insert in the hydrophobic region of the membrane where the peptide has adequate conditions to achieve the oligomerization.Fil: Castellano, Patricia Haydee. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; ArgentinaFil: Vignolo, Graciela Margarita. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; ArgentinaFil: Farias, Ricardo Norberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Arrondo Jose Luis. Universidad Politécnica de Valencia; EspañaFil: Chehin, Rosana Nieves. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaAmerican Society for Microbiology2007-01-20info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/56340Castellano, Patricia Haydee; Vignolo, Graciela Margarita; Farias, Ricardo Norberto; Arrondo Jose Luis; Chehin, Rosana Nieves; Molecular view by Fourier transform infrared spectroscopy of the relationship between lactocin 705 and membranes: Speculations on antimicrobial mechanism; American Society for Microbiology; Applied And Environmental Microbiology; 73; 2; 20-1-2007; 415-4200099-22401098-5336CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1128/AEM.01293-06info:eu-repo/semantics/altIdentifier/url/https://aem.asm.org/content/73/2/415info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:12:47Zoai:ri.conicet.gov.ar:11336/56340instacron: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 10:12:47.384CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Molecular view by Fourier transform infrared spectroscopy of the relationship between lactocin 705 and membranes: Speculations on antimicrobial mechanism |
title |
Molecular view by Fourier transform infrared spectroscopy of the relationship between lactocin 705 and membranes: Speculations on antimicrobial mechanism |
spellingShingle |
Molecular view by Fourier transform infrared spectroscopy of the relationship between lactocin 705 and membranes: Speculations on antimicrobial mechanism Castellano, Patricia Haydee Antimicrobial Peptide Lactocin 705 Mechanism of Action Ftir Fourier Transform Infrared Spectroscopy |
title_short |
Molecular view by Fourier transform infrared spectroscopy of the relationship between lactocin 705 and membranes: Speculations on antimicrobial mechanism |
title_full |
Molecular view by Fourier transform infrared spectroscopy of the relationship between lactocin 705 and membranes: Speculations on antimicrobial mechanism |
title_fullStr |
Molecular view by Fourier transform infrared spectroscopy of the relationship between lactocin 705 and membranes: Speculations on antimicrobial mechanism |
title_full_unstemmed |
Molecular view by Fourier transform infrared spectroscopy of the relationship between lactocin 705 and membranes: Speculations on antimicrobial mechanism |
title_sort |
Molecular view by Fourier transform infrared spectroscopy of the relationship between lactocin 705 and membranes: Speculations on antimicrobial mechanism |
dc.creator.none.fl_str_mv |
Castellano, Patricia Haydee Vignolo, Graciela Margarita Farias, Ricardo Norberto Arrondo Jose Luis Chehin, Rosana Nieves |
author |
Castellano, Patricia Haydee |
author_facet |
Castellano, Patricia Haydee Vignolo, Graciela Margarita Farias, Ricardo Norberto Arrondo Jose Luis Chehin, Rosana Nieves |
author_role |
author |
author2 |
Vignolo, Graciela Margarita Farias, Ricardo Norberto Arrondo Jose Luis Chehin, Rosana Nieves |
author2_role |
author author author author |
dc.subject.none.fl_str_mv |
Antimicrobial Peptide Lactocin 705 Mechanism of Action Ftir Fourier Transform Infrared Spectroscopy |
topic |
Antimicrobial Peptide Lactocin 705 Mechanism of Action Ftir Fourier Transform Infrared Spectroscopy |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Lactocin 705 is a bacteriocin whose activity depends upon the complementation of two peptides, termed Lac705α and Lac705β. Neither Lac705α nor Lac705β displayed bacteriocin activity by itself when the growth of sensitive cells was monitored. To obtain molecular insights into the lactocin 705 mechanism of action, Fourier transform infrared spectroscopy was used to investigate the interactions of each peptide (Lac705α and Lac705β) with dipalmitoylphosphatidylcholine liposomal membranes. Both peptides show the ability to interact with the zwitterionic membrane but at different bilayer levels. While Lac705α interacts with the interfacial region inducing dehydration, Lac705β peptide interacts with only the hydrophobic core. This paper presents the first experimental evidence that supports the hypothesis that Lac705α and Lac705β peptides could form a transmembrane oligomer. From the obtained results, a mechanism of action of lactocin 705 on membrane systems is proposed. The component Lac705α could induce the dehydration of the bilayer interfacial region, and the Lac705β peptide could insert in the hydrophobic region of the membrane where the peptide has adequate conditions to achieve the oligomerization. Fil: Castellano, Patricia Haydee. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina Fil: Vignolo, Graciela Margarita. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Centro de Referencia para Lactobacilos; Argentina Fil: Farias, Ricardo Norberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina Fil: Arrondo Jose Luis. Universidad Politécnica de Valencia; España Fil: Chehin, Rosana Nieves. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina |
description |
Lactocin 705 is a bacteriocin whose activity depends upon the complementation of two peptides, termed Lac705α and Lac705β. Neither Lac705α nor Lac705β displayed bacteriocin activity by itself when the growth of sensitive cells was monitored. To obtain molecular insights into the lactocin 705 mechanism of action, Fourier transform infrared spectroscopy was used to investigate the interactions of each peptide (Lac705α and Lac705β) with dipalmitoylphosphatidylcholine liposomal membranes. Both peptides show the ability to interact with the zwitterionic membrane but at different bilayer levels. While Lac705α interacts with the interfacial region inducing dehydration, Lac705β peptide interacts with only the hydrophobic core. This paper presents the first experimental evidence that supports the hypothesis that Lac705α and Lac705β peptides could form a transmembrane oligomer. From the obtained results, a mechanism of action of lactocin 705 on membrane systems is proposed. The component Lac705α could induce the dehydration of the bilayer interfacial region, and the Lac705β peptide could insert in the hydrophobic region of the membrane where the peptide has adequate conditions to achieve the oligomerization. |
publishDate |
2007 |
dc.date.none.fl_str_mv |
2007-01-20 |
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/11336/56340 Castellano, Patricia Haydee; Vignolo, Graciela Margarita; Farias, Ricardo Norberto; Arrondo Jose Luis; Chehin, Rosana Nieves; Molecular view by Fourier transform infrared spectroscopy of the relationship between lactocin 705 and membranes: Speculations on antimicrobial mechanism; American Society for Microbiology; Applied And Environmental Microbiology; 73; 2; 20-1-2007; 415-420 0099-2240 1098-5336 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/56340 |
identifier_str_mv |
Castellano, Patricia Haydee; Vignolo, Graciela Margarita; Farias, Ricardo Norberto; Arrondo Jose Luis; Chehin, Rosana Nieves; Molecular view by Fourier transform infrared spectroscopy of the relationship between lactocin 705 and membranes: Speculations on antimicrobial mechanism; American Society for Microbiology; Applied And Environmental Microbiology; 73; 2; 20-1-2007; 415-420 0099-2240 1098-5336 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1128/AEM.01293-06 info:eu-repo/semantics/altIdentifier/url/https://aem.asm.org/content/73/2/415 |
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 |
dc.publisher.none.fl_str_mv |
American Society for Microbiology |
publisher.none.fl_str_mv |
American Society for Microbiology |
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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1844614037542797312 |
score |
13.070432 |