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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/56340
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/56340
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling 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 Técnicas2025-10-22T11:42:40Zoai: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:34982025-10-22 11:42:40.357CONICET 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
_version_ 1846782114716975104
score 12.982451

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