Surface mixing of products and substrate of PLA2 in enzyme-free mixed monolayers reproduces enzyme-driven structural topography

Autores
de Tullio, Luisina; Fanani, Maria Laura; Maggio, Bruno
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
It was proposed that topographic changes in lipid monolayers hydrolyzed by lipolytic enzymes such as Phospholipase A2 (PLA2) are a consequence of enzyme activity at the surface. Lateral packing defects that arise from lipid phase coexistence were suggested as places at which PLA2 activity is preferably localized. Our work employs a method for mixing two lipid monolayers in order to simulate lipid mixing of products and substrate at the surface in the absence of enzyme. In such enzyme-free mixed films, a topographic pattern similar to that actively generated by PLA2 is observed. The main conclusion from our experiments is that mixing–demixing properties of substrate and products generated by PLA2 can determine the evolution of the surface topography.
Fil: de Tullio, Luisina. 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 Cs.químicas. Centro de Investigaciones En Química Biológica de Córdoba; Argentina
Fil: Fanani, Maria Laura. 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 Cs.químicas. Centro de Investigaciones En Química Biológica de Córdoba; Argentina
Fil: Maggio, Bruno. 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 Cs.químicas. Centro de Investigaciones En Química Biológica de Córdoba; Argentina
Materia
Porcine Pancreas Phospholipase A2
Dipalmitoylphosphatidylcholine
Lipid Monolayer
Lipid Domain Morphology
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:11336/25408
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Surface mixing of products and substrate of PLA2 in enzyme-free mixed monolayers reproduces enzyme-driven structural topographyde Tullio, LuisinaFanani, Maria LauraMaggio, BrunoPorcine Pancreas Phospholipase A2DipalmitoylphosphatidylcholineLipid MonolayerLipid Domain Morphologyhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1It was proposed that topographic changes in lipid monolayers hydrolyzed by lipolytic enzymes such as Phospholipase A2 (PLA2) are a consequence of enzyme activity at the surface. Lateral packing defects that arise from lipid phase coexistence were suggested as places at which PLA2 activity is preferably localized. Our work employs a method for mixing two lipid monolayers in order to simulate lipid mixing of products and substrate at the surface in the absence of enzyme. In such enzyme-free mixed films, a topographic pattern similar to that actively generated by PLA2 is observed. The main conclusion from our experiments is that mixing–demixing properties of substrate and products generated by PLA2 can determine the evolution of the surface topography.Fil: de Tullio, Luisina. 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 Cs.químicas. Centro de Investigaciones En Química Biológica de Córdoba; ArgentinaFil: Fanani, Maria Laura. 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 Cs.químicas. Centro de Investigaciones En Química Biológica de Córdoba; ArgentinaFil: Maggio, Bruno. 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 Cs.químicas. Centro de Investigaciones En Química Biológica de Córdoba; ArgentinaElsevier Science2013-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/25408de Tullio, Luisina; Fanani, Maria Laura; Maggio, Bruno; Surface mixing of products and substrate of PLA2 in enzyme-free mixed monolayers reproduces enzyme-driven structural topography; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1828; 9; 5-2013; 2056-20630005-2736CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2013.05.018info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0005273613001648info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:42:59Zoai:ri.conicet.gov.ar:11336/25408instacron: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 14:42:59.707CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Surface mixing of products and substrate of PLA2 in enzyme-free mixed monolayers reproduces enzyme-driven structural topography
title Surface mixing of products and substrate of PLA2 in enzyme-free mixed monolayers reproduces enzyme-driven structural topography
spellingShingle Surface mixing of products and substrate of PLA2 in enzyme-free mixed monolayers reproduces enzyme-driven structural topography
de Tullio, Luisina
Porcine Pancreas Phospholipase A2
Dipalmitoylphosphatidylcholine
Lipid Monolayer
Lipid Domain Morphology
title_short Surface mixing of products and substrate of PLA2 in enzyme-free mixed monolayers reproduces enzyme-driven structural topography
title_full Surface mixing of products and substrate of PLA2 in enzyme-free mixed monolayers reproduces enzyme-driven structural topography
title_fullStr Surface mixing of products and substrate of PLA2 in enzyme-free mixed monolayers reproduces enzyme-driven structural topography
title_full_unstemmed Surface mixing of products and substrate of PLA2 in enzyme-free mixed monolayers reproduces enzyme-driven structural topography
title_sort Surface mixing of products and substrate of PLA2 in enzyme-free mixed monolayers reproduces enzyme-driven structural topography
dc.creator.none.fl_str_mv de Tullio, Luisina
Fanani, Maria Laura
Maggio, Bruno
author de Tullio, Luisina
author_facet de Tullio, Luisina
Fanani, Maria Laura
Maggio, Bruno
author_role author
author2 Fanani, Maria Laura
Maggio, Bruno
author2_role author
author
dc.subject.none.fl_str_mv Porcine Pancreas Phospholipase A2
Dipalmitoylphosphatidylcholine
Lipid Monolayer
Lipid Domain Morphology
topic Porcine Pancreas Phospholipase A2
Dipalmitoylphosphatidylcholine
Lipid Monolayer
Lipid Domain Morphology
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv It was proposed that topographic changes in lipid monolayers hydrolyzed by lipolytic enzymes such as Phospholipase A2 (PLA2) are a consequence of enzyme activity at the surface. Lateral packing defects that arise from lipid phase coexistence were suggested as places at which PLA2 activity is preferably localized. Our work employs a method for mixing two lipid monolayers in order to simulate lipid mixing of products and substrate at the surface in the absence of enzyme. In such enzyme-free mixed films, a topographic pattern similar to that actively generated by PLA2 is observed. The main conclusion from our experiments is that mixing–demixing properties of substrate and products generated by PLA2 can determine the evolution of the surface topography.
Fil: de Tullio, Luisina. 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 Cs.químicas. Centro de Investigaciones En Química Biológica de Córdoba; Argentina
Fil: Fanani, Maria Laura. 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 Cs.químicas. Centro de Investigaciones En Química Biológica de Córdoba; Argentina
Fil: Maggio, Bruno. 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 Cs.químicas. Centro de Investigaciones En Química Biológica de Córdoba; Argentina
description It was proposed that topographic changes in lipid monolayers hydrolyzed by lipolytic enzymes such as Phospholipase A2 (PLA2) are a consequence of enzyme activity at the surface. Lateral packing defects that arise from lipid phase coexistence were suggested as places at which PLA2 activity is preferably localized. Our work employs a method for mixing two lipid monolayers in order to simulate lipid mixing of products and substrate at the surface in the absence of enzyme. In such enzyme-free mixed films, a topographic pattern similar to that actively generated by PLA2 is observed. The main conclusion from our experiments is that mixing–demixing properties of substrate and products generated by PLA2 can determine the evolution of the surface topography.
publishDate 2013
dc.date.none.fl_str_mv 2013-05
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/11336/25408
de Tullio, Luisina; Fanani, Maria Laura; Maggio, Bruno; Surface mixing of products and substrate of PLA2 in enzyme-free mixed monolayers reproduces enzyme-driven structural topography; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1828; 9; 5-2013; 2056-2063
0005-2736
CONICET Digital
CONICET
url http://hdl.handle.net/11336/25408
identifier_str_mv de Tullio, Luisina; Fanani, Maria Laura; Maggio, Bruno; Surface mixing of products and substrate of PLA2 in enzyme-free mixed monolayers reproduces enzyme-driven structural topography; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1828; 9; 5-2013; 2056-2063
0005-2736
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2013.05.018
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0005273613001648
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 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
_version_ 1846082933769633792
score 13.22299

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