Interaction of the antibiotic peptide nisin with anionic membranes in different phase-states: A vibrational study

Autores
Sosa Morales, Marcelo Clemente; Juárez, Ana Carolina; Montich, Guillermo Gabriel; Alvarez, Rosa Maria Susana
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Interactions between the antibiotic peptide nisin and multilamellar vesicles of phosphoglycerol lipids in different phase-states were studied using vibrational spectroscopy. The infrared amide I′ band of nisin, both in solution and in the membrane-bound state, was analyzed in the temperature range comprised between 20 and 60 °C in order to study its conformational behavior. Nisin presented mainly unordered and β-turns conformations. Their relative populations varied according to the environment and as the temperature increased: β turns were more favored in the membrane-bound state than in solution, but at higher temperatures the disordered conformation was dominant in both states. Spectral changes of specific infrared bands belonging to the hydrocarbon and polar moieties of lipids were also analyzed to evaluate the perturbation of the lipid membrane order. Nisin interactions with the membrane polar region induced a high restriction to water incorporation, promoting a small increase in the temperature of the lipid phase transition. Raman spectra of nisin/phosphoglycerol systems at ambient temperature were also analyzed. They revealed that the peptide incorporation to a membrane in the fluid phase caused drastic structural modifications in the hydrophobic region of the bilayer. Although nisin may be able to disrupt the hydrophobic portion of the bilayer in the gel phase, the most of the peptide molecule remained at the membrane surface interacting with the polar headgroups. This work provides evidence of a differential effect of nisin on anionic membranes, depending on the phase-state of the lipid.
Fil: Sosa Morales, Marcelo Clemente. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
Fil: Juárez, Ana Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
Fil: Montich, Guillermo Gabriel. 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: Alvarez, Rosa Maria Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
Materia
ANIONIC MEMBRANES
NISIN
VIBRATIONAL 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:11336/106764
Acceder
id CONICETDig_d17f92a9070d6100435463270ca046fa
oai_identifier_str oai:ri.conicet.gov.ar:11336/106764
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Interaction of the antibiotic peptide nisin with anionic membranes in different phase-states: A vibrational studySosa Morales, Marcelo ClementeJuárez, Ana CarolinaMontich, Guillermo GabrielAlvarez, Rosa Maria SusanaANIONIC MEMBRANESNISINVIBRATIONAL SPECTROSCOPYhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Interactions between the antibiotic peptide nisin and multilamellar vesicles of phosphoglycerol lipids in different phase-states were studied using vibrational spectroscopy. The infrared amide I′ band of nisin, both in solution and in the membrane-bound state, was analyzed in the temperature range comprised between 20 and 60 °C in order to study its conformational behavior. Nisin presented mainly unordered and β-turns conformations. Their relative populations varied according to the environment and as the temperature increased: β turns were more favored in the membrane-bound state than in solution, but at higher temperatures the disordered conformation was dominant in both states. Spectral changes of specific infrared bands belonging to the hydrocarbon and polar moieties of lipids were also analyzed to evaluate the perturbation of the lipid membrane order. Nisin interactions with the membrane polar region induced a high restriction to water incorporation, promoting a small increase in the temperature of the lipid phase transition. Raman spectra of nisin/phosphoglycerol systems at ambient temperature were also analyzed. They revealed that the peptide incorporation to a membrane in the fluid phase caused drastic structural modifications in the hydrophobic region of the bilayer. Although nisin may be able to disrupt the hydrophobic portion of the bilayer in the gel phase, the most of the peptide molecule remained at the membrane surface interacting with the polar headgroups. This work provides evidence of a differential effect of nisin on anionic membranes, depending on the phase-state of the lipid.Fil: Sosa Morales, Marcelo Clemente. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; ArgentinaFil: Juárez, Ana Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; ArgentinaFil: Montich, Guillermo Gabriel. 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: Alvarez, Rosa Maria Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; ArgentinaPergamon-Elsevier Science Ltd2019-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/106764Sosa Morales, Marcelo Clemente; Juárez, Ana Carolina; Montich, Guillermo Gabriel; Alvarez, Rosa Maria Susana; Interaction of the antibiotic peptide nisin with anionic membranes in different phase-states: A vibrational study; Pergamon-Elsevier Science Ltd; Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy; 215; 5-2019; 389-3971386-1425CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S1386142519302409info:eu-repo/semantics/altIdentifier/doi/10.1016/j.saa.2019.03.009info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-17T11:31:50Zoai:ri.conicet.gov.ar:11336/106764instacron: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:34982025-09-17 11:31:50.619CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Interaction of the antibiotic peptide nisin with anionic membranes in different phase-states: A vibrational study
title Interaction of the antibiotic peptide nisin with anionic membranes in different phase-states: A vibrational study
spellingShingle Interaction of the antibiotic peptide nisin with anionic membranes in different phase-states: A vibrational study
Sosa Morales, Marcelo Clemente
ANIONIC MEMBRANES
NISIN
VIBRATIONAL SPECTROSCOPY
title_short Interaction of the antibiotic peptide nisin with anionic membranes in different phase-states: A vibrational study
title_full Interaction of the antibiotic peptide nisin with anionic membranes in different phase-states: A vibrational study
title_fullStr Interaction of the antibiotic peptide nisin with anionic membranes in different phase-states: A vibrational study
title_full_unstemmed Interaction of the antibiotic peptide nisin with anionic membranes in different phase-states: A vibrational study
title_sort Interaction of the antibiotic peptide nisin with anionic membranes in different phase-states: A vibrational study
dc.creator.none.fl_str_mv Sosa Morales, Marcelo Clemente
Juárez, Ana Carolina
Montich, Guillermo Gabriel
Alvarez, Rosa Maria Susana
author Sosa Morales, Marcelo Clemente
author_facet Sosa Morales, Marcelo Clemente
Juárez, Ana Carolina
Montich, Guillermo Gabriel
Alvarez, Rosa Maria Susana
author_role author
author2 Juárez, Ana Carolina
Montich, Guillermo Gabriel
Alvarez, Rosa Maria Susana
author2_role author
author
author
dc.subject.none.fl_str_mv ANIONIC MEMBRANES
NISIN
VIBRATIONAL SPECTROSCOPY
topic ANIONIC MEMBRANES
NISIN
VIBRATIONAL SPECTROSCOPY
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Interactions between the antibiotic peptide nisin and multilamellar vesicles of phosphoglycerol lipids in different phase-states were studied using vibrational spectroscopy. The infrared amide I′ band of nisin, both in solution and in the membrane-bound state, was analyzed in the temperature range comprised between 20 and 60 °C in order to study its conformational behavior. Nisin presented mainly unordered and β-turns conformations. Their relative populations varied according to the environment and as the temperature increased: β turns were more favored in the membrane-bound state than in solution, but at higher temperatures the disordered conformation was dominant in both states. Spectral changes of specific infrared bands belonging to the hydrocarbon and polar moieties of lipids were also analyzed to evaluate the perturbation of the lipid membrane order. Nisin interactions with the membrane polar region induced a high restriction to water incorporation, promoting a small increase in the temperature of the lipid phase transition. Raman spectra of nisin/phosphoglycerol systems at ambient temperature were also analyzed. They revealed that the peptide incorporation to a membrane in the fluid phase caused drastic structural modifications in the hydrophobic region of the bilayer. Although nisin may be able to disrupt the hydrophobic portion of the bilayer in the gel phase, the most of the peptide molecule remained at the membrane surface interacting with the polar headgroups. This work provides evidence of a differential effect of nisin on anionic membranes, depending on the phase-state of the lipid.
Fil: Sosa Morales, Marcelo Clemente. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
Fil: Juárez, Ana Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
Fil: Montich, Guillermo Gabriel. 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: Alvarez, Rosa Maria Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
description Interactions between the antibiotic peptide nisin and multilamellar vesicles of phosphoglycerol lipids in different phase-states were studied using vibrational spectroscopy. The infrared amide I′ band of nisin, both in solution and in the membrane-bound state, was analyzed in the temperature range comprised between 20 and 60 °C in order to study its conformational behavior. Nisin presented mainly unordered and β-turns conformations. Their relative populations varied according to the environment and as the temperature increased: β turns were more favored in the membrane-bound state than in solution, but at higher temperatures the disordered conformation was dominant in both states. Spectral changes of specific infrared bands belonging to the hydrocarbon and polar moieties of lipids were also analyzed to evaluate the perturbation of the lipid membrane order. Nisin interactions with the membrane polar region induced a high restriction to water incorporation, promoting a small increase in the temperature of the lipid phase transition. Raman spectra of nisin/phosphoglycerol systems at ambient temperature were also analyzed. They revealed that the peptide incorporation to a membrane in the fluid phase caused drastic structural modifications in the hydrophobic region of the bilayer. Although nisin may be able to disrupt the hydrophobic portion of the bilayer in the gel phase, the most of the peptide molecule remained at the membrane surface interacting with the polar headgroups. This work provides evidence of a differential effect of nisin on anionic membranes, depending on the phase-state of the lipid.
publishDate 2019
dc.date.none.fl_str_mv 2019-05
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/11336/106764
Sosa Morales, Marcelo Clemente; Juárez, Ana Carolina; Montich, Guillermo Gabriel; Alvarez, Rosa Maria Susana; Interaction of the antibiotic peptide nisin with anionic membranes in different phase-states: A vibrational study; Pergamon-Elsevier Science Ltd; Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy; 215; 5-2019; 389-397
1386-1425
CONICET Digital
CONICET
url http://hdl.handle.net/11336/106764
identifier_str_mv Sosa Morales, Marcelo Clemente; Juárez, Ana Carolina; Montich, Guillermo Gabriel; Alvarez, Rosa Maria Susana; Interaction of the antibiotic peptide nisin with anionic membranes in different phase-states: A vibrational study; Pergamon-Elsevier Science Ltd; Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy; 215; 5-2019; 389-397
1386-1425
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.sciencedirect.com/science/article/abs/pii/S1386142519302409
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.saa.2019.03.009
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
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Pergamon-Elsevier Science Ltd
publisher.none.fl_str_mv Pergamon-Elsevier Science Ltd
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_ 1843606677765488640
score 13.001348

Publicaciones similares