Possible mechanism of structural transformations induced by StAsp-PSI in lipid membranes

Autores
Muñoz, Fernando Felipe; Palomares Jerez, M. Francisca; Daleo, Gustavo Raul; Villalaín, José; Guevara, Maria Gabriela
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In the present work we have analyzed the effect of StAsp-PSI (plant-specific insert of potato aspartic protease) on the structural and thermotropic properties of the major phospholipid types of bacterial and animal cells. Results obtained suggest that StAsp-PSI induces a destabilization of the membrane bilayers, depending on the time of interaction between the protein and the bilayers, rather than on its concentration. This temporal delay would be consistent with a lateral diffusion of StAsp-PSI monomers to assemble into aggregates to form pores. Like with the results previously reported for the StAsp-PSI circular dichroism, data obtained here from IR spectroscopy show that there are slight changes in the StAsp-PSI secondary structure in the presence of lipid membranes; suggesting that these changes could be related with the StAsp-PSI self-association. Results obtained from steady-state fluorescence anisotropy and differential scanning calorimetry assays suggest that StAsp-PSI interacts with both uncharged and negatively charged phospholipids, modulates the phase polymorphic behavior of model membranes and partitions and buries differentially in the membrane depending on the presence of negatively charged phospholipids.
Fil: Muñoz, Fernando Felipe. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; Argentina
Fil: Palomares Jerez, M. Francisca . Universidad de Miguel Hernandez; España
Fil: Daleo, Gustavo Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; Argentina
Fil: Villalaín, José . Universidad de Miguel Hernandez; España
Fil: Guevara, Maria Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; Argentina
Materia
Antimicrobial Protein
Antitumor Protein
Plant Aspartic Protease
Plant-Specific Insert
Membrane Destabilization
Α-Helix
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/13052
Acceder
id CONICETDig_47165a969ea85941d298364b619d7e9a
oai_identifier_str oai:ri.conicet.gov.ar:11336/13052
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Possible mechanism of structural transformations induced by StAsp-PSI in lipid membranesMuñoz, Fernando FelipePalomares Jerez, M. Francisca Daleo, Gustavo RaulVillalaín, José Guevara, Maria GabrielaAntimicrobial ProteinAntitumor ProteinPlant Aspartic ProteasePlant-Specific InsertMembrane DestabilizationΑ-Helixhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1In the present work we have analyzed the effect of StAsp-PSI (plant-specific insert of potato aspartic protease) on the structural and thermotropic properties of the major phospholipid types of bacterial and animal cells. Results obtained suggest that StAsp-PSI induces a destabilization of the membrane bilayers, depending on the time of interaction between the protein and the bilayers, rather than on its concentration. This temporal delay would be consistent with a lateral diffusion of StAsp-PSI monomers to assemble into aggregates to form pores. Like with the results previously reported for the StAsp-PSI circular dichroism, data obtained here from IR spectroscopy show that there are slight changes in the StAsp-PSI secondary structure in the presence of lipid membranes; suggesting that these changes could be related with the StAsp-PSI self-association. Results obtained from steady-state fluorescence anisotropy and differential scanning calorimetry assays suggest that StAsp-PSI interacts with both uncharged and negatively charged phospholipids, modulates the phase polymorphic behavior of model membranes and partitions and buries differentially in the membrane depending on the presence of negatively charged phospholipids.Fil: Muñoz, Fernando Felipe. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; ArgentinaFil: Palomares Jerez, M. Francisca . Universidad de Miguel Hernandez; EspañaFil: Daleo, Gustavo Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; ArgentinaFil: Villalaín, José . Universidad de Miguel Hernandez; EspañaFil: Guevara, Maria Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; ArgentinaElsevier Science2014-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/13052Muñoz, Fernando Felipe; Palomares Jerez, M. Francisca ; Daleo, Gustavo Raul; Villalaín, José ; Guevara, Maria Gabriela; Possible mechanism of structural transformations induced by StAsp-PSI in lipid membranes; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1838; 1B; 1-2014; 339-3470005-2736enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0005273613002812info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2013.08.004info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:41:00Zoai:ri.conicet.gov.ar:11336/13052instacron: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:34982025-10-15 14:41:00.627CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Possible mechanism of structural transformations induced by StAsp-PSI in lipid membranes
title Possible mechanism of structural transformations induced by StAsp-PSI in lipid membranes
spellingShingle Possible mechanism of structural transformations induced by StAsp-PSI in lipid membranes
Muñoz, Fernando Felipe
Antimicrobial Protein
Antitumor Protein
Plant Aspartic Protease
Plant-Specific Insert
Membrane Destabilization
Α-Helix
title_short Possible mechanism of structural transformations induced by StAsp-PSI in lipid membranes
title_full Possible mechanism of structural transformations induced by StAsp-PSI in lipid membranes
title_fullStr Possible mechanism of structural transformations induced by StAsp-PSI in lipid membranes
title_full_unstemmed Possible mechanism of structural transformations induced by StAsp-PSI in lipid membranes
title_sort Possible mechanism of structural transformations induced by StAsp-PSI in lipid membranes
dc.creator.none.fl_str_mv Muñoz, Fernando Felipe
Palomares Jerez, M. Francisca
Daleo, Gustavo Raul
Villalaín, José
Guevara, Maria Gabriela
author Muñoz, Fernando Felipe
author_facet Muñoz, Fernando Felipe
Palomares Jerez, M. Francisca
Daleo, Gustavo Raul
Villalaín, José
Guevara, Maria Gabriela
author_role author
author2 Palomares Jerez, M. Francisca
Daleo, Gustavo Raul
Villalaín, José
Guevara, Maria Gabriela
author2_role author
author
author
author
dc.subject.none.fl_str_mv Antimicrobial Protein
Antitumor Protein
Plant Aspartic Protease
Plant-Specific Insert
Membrane Destabilization
Α-Helix
topic Antimicrobial Protein
Antitumor Protein
Plant Aspartic Protease
Plant-Specific Insert
Membrane Destabilization
Α-Helix
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv In the present work we have analyzed the effect of StAsp-PSI (plant-specific insert of potato aspartic protease) on the structural and thermotropic properties of the major phospholipid types of bacterial and animal cells. Results obtained suggest that StAsp-PSI induces a destabilization of the membrane bilayers, depending on the time of interaction between the protein and the bilayers, rather than on its concentration. This temporal delay would be consistent with a lateral diffusion of StAsp-PSI monomers to assemble into aggregates to form pores. Like with the results previously reported for the StAsp-PSI circular dichroism, data obtained here from IR spectroscopy show that there are slight changes in the StAsp-PSI secondary structure in the presence of lipid membranes; suggesting that these changes could be related with the StAsp-PSI self-association. Results obtained from steady-state fluorescence anisotropy and differential scanning calorimetry assays suggest that StAsp-PSI interacts with both uncharged and negatively charged phospholipids, modulates the phase polymorphic behavior of model membranes and partitions and buries differentially in the membrane depending on the presence of negatively charged phospholipids.
Fil: Muñoz, Fernando Felipe. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; Argentina
Fil: Palomares Jerez, M. Francisca . Universidad de Miguel Hernandez; España
Fil: Daleo, Gustavo Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; Argentina
Fil: Villalaín, José . Universidad de Miguel Hernandez; España
Fil: Guevara, Maria Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; Argentina
description In the present work we have analyzed the effect of StAsp-PSI (plant-specific insert of potato aspartic protease) on the structural and thermotropic properties of the major phospholipid types of bacterial and animal cells. Results obtained suggest that StAsp-PSI induces a destabilization of the membrane bilayers, depending on the time of interaction between the protein and the bilayers, rather than on its concentration. This temporal delay would be consistent with a lateral diffusion of StAsp-PSI monomers to assemble into aggregates to form pores. Like with the results previously reported for the StAsp-PSI circular dichroism, data obtained here from IR spectroscopy show that there are slight changes in the StAsp-PSI secondary structure in the presence of lipid membranes; suggesting that these changes could be related with the StAsp-PSI self-association. Results obtained from steady-state fluorescence anisotropy and differential scanning calorimetry assays suggest that StAsp-PSI interacts with both uncharged and negatively charged phospholipids, modulates the phase polymorphic behavior of model membranes and partitions and buries differentially in the membrane depending on the presence of negatively charged phospholipids.
publishDate 2014
dc.date.none.fl_str_mv 2014-01
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/11336/13052
Muñoz, Fernando Felipe; Palomares Jerez, M. Francisca ; Daleo, Gustavo Raul; Villalaín, José ; Guevara, Maria Gabriela; Possible mechanism of structural transformations induced by StAsp-PSI in lipid membranes; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1838; 1B; 1-2014; 339-347
0005-2736
url http://hdl.handle.net/11336/13052
identifier_str_mv Muñoz, Fernando Felipe; Palomares Jerez, M. Francisca ; Daleo, Gustavo Raul; Villalaín, José ; Guevara, Maria Gabriela; Possible mechanism of structural transformations induced by StAsp-PSI in lipid membranes; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1838; 1B; 1-2014; 339-347
0005-2736
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0005273613002812
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2013.08.004
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
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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score 13.22299

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