Molecular view by fourier transform infrared spectroscopy of the relationship between lactocin 705 and membranes: speculations on antimicrobial mechanism
- Autores
- Farias, Ricardo Norberto; Castellano, Patricia; Vignolo, Graciela Margarita; Arrondo, José 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 Lac705alpha and Lac705beta. Neither Lac705alpha nor Lac705beta 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 (Lac705alpha and Lac705beta) with dipalmitoylphosphatidylcholine liposomal membranes. Both peptides show the ability to interact with the zwitterionic membrane but at different bilayer levels. While Lac705alpha interacts with the interfacial region inducing dehydration, Lac705beta peptide interacts with only the hydrophobic core. This paper presents the first experimental evidence that supports the hypothesis that Lac705alpha and Lac705beta peptides could form a transmembrane oligomer. From the obtained results, a mechanism of action of lactocin 705 on membrane systems is proposed. The component Lac705alpha could induce the dehydration of the bilayer interfacial region, and the Lac705beta peptide could insert in the hydrophobic region of the membrane where the peptide has adequate conditions to achieve the oligomerization.
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: Castellano, Patricia. 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: Arrondo, José Luis. Consejo Superior de Investigaciones Científicas; 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 - 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:11336/82975
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 mechanismFarias, Ricardo NorbertoCastellano, PatriciaVignolo, Graciela MargaritaArrondo, José LuisChehin, Rosana Nieveshttps://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 Lac705alpha and Lac705beta. Neither Lac705alpha nor Lac705beta 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 (Lac705alpha and Lac705beta) with dipalmitoylphosphatidylcholine liposomal membranes. Both peptides show the ability to interact with the zwitterionic membrane but at different bilayer levels. While Lac705alpha interacts with the interfacial region inducing dehydration, Lac705beta peptide interacts with only the hydrophobic core. This paper presents the first experimental evidence that supports the hypothesis that Lac705alpha and Lac705beta peptides could form a transmembrane oligomer. From the obtained results, a mechanism of action of lactocin 705 on membrane systems is proposed. The component Lac705alpha could induce the dehydration of the bilayer interfacial region, and the Lac705beta peptide could insert in the hydrophobic region of the membrane where the peptide has adequate conditions to achieve the oligomerization.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; ArgentinaFil: Castellano, Patricia. 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: Arrondo, José Luis. Consejo Superior de Investigaciones Científicas; 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 Microbiology2007-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/82975Farias, Ricardo Norberto; Castellano, Patricia; Vignolo, Graciela Margarita; Arrondo, José 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; 12-2007; 415-4200099-2240CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1128/AEM.01293-06info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pubmed/17071790info:eu-repo/semantics/altIdentifier/url/https://aem.asm.org/content/73/2/415/article-infoinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:50:52Zoai:ri.conicet.gov.ar:11336/82975instacron: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 09:50:52.726CONICET 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 Farias, Ricardo Norberto |
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 |
Farias, Ricardo Norberto Castellano, Patricia Vignolo, Graciela Margarita Arrondo, José Luis Chehin, Rosana Nieves |
author |
Farias, Ricardo Norberto |
author_facet |
Farias, Ricardo Norberto Castellano, Patricia Vignolo, Graciela Margarita Arrondo, José Luis Chehin, Rosana Nieves |
author_role |
author |
author2 |
Castellano, Patricia Vignolo, Graciela Margarita Arrondo, José Luis Chehin, Rosana Nieves |
author2_role |
author author author author |
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 Lac705alpha and Lac705beta. Neither Lac705alpha nor Lac705beta 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 (Lac705alpha and Lac705beta) with dipalmitoylphosphatidylcholine liposomal membranes. Both peptides show the ability to interact with the zwitterionic membrane but at different bilayer levels. While Lac705alpha interacts with the interfacial region inducing dehydration, Lac705beta peptide interacts with only the hydrophobic core. This paper presents the first experimental evidence that supports the hypothesis that Lac705alpha and Lac705beta peptides could form a transmembrane oligomer. From the obtained results, a mechanism of action of lactocin 705 on membrane systems is proposed. The component Lac705alpha could induce the dehydration of the bilayer interfacial region, and the Lac705beta peptide could insert in the hydrophobic region of the membrane where the peptide has adequate conditions to achieve the oligomerization. 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: Castellano, Patricia. 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: Arrondo, José Luis. Consejo Superior de Investigaciones Científicas; 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 Lac705alpha and Lac705beta. Neither Lac705alpha nor Lac705beta 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 (Lac705alpha and Lac705beta) with dipalmitoylphosphatidylcholine liposomal membranes. Both peptides show the ability to interact with the zwitterionic membrane but at different bilayer levels. While Lac705alpha interacts with the interfacial region inducing dehydration, Lac705beta peptide interacts with only the hydrophobic core. This paper presents the first experimental evidence that supports the hypothesis that Lac705alpha and Lac705beta peptides could form a transmembrane oligomer. From the obtained results, a mechanism of action of lactocin 705 on membrane systems is proposed. The component Lac705alpha could induce the dehydration of the bilayer interfacial region, and the Lac705beta 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 |
2007-12 |
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/11336/82975 Farias, Ricardo Norberto; Castellano, Patricia; Vignolo, Graciela Margarita; Arrondo, José 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; 12-2007; 415-420 0099-2240 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/82975 |
identifier_str_mv |
Farias, Ricardo Norberto; Castellano, Patricia; Vignolo, Graciela Margarita; Arrondo, José 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; 12-2007; 415-420 0099-2240 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://www.ncbi.nlm.nih.gov/pubmed/17071790 info:eu-repo/semantics/altIdentifier/url/https://aem.asm.org/content/73/2/415/article-info |
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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1844613566975442944 |
score |
13.070432 |