Protein nanorotors control the size of lipid domains in phase-separated monolayers

Autores
Carrillo Godoy, Nuria; Valdivieso González, David; Natale, Paolo; Ritacco, Hernán Alejandro; Cao García, Francisco J.; Almendro Vedia, Víctor G.; López Montero, Iván
Año de publicación
2025
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Hypothesis: Phase separation in lipid membranes leads to the formation of distinct lipid domains, which are influenced by kinetic factors and interfacial phenomena. While line tension has been considered a key determinant of domain size, studies suggest that kinetic effects play a significant role. We hypothesize that modifying in situ the surface pressure difference between coexisting lipid phases can regulate domain size. Specifically, the rotational activity of ATP synthase embedded in a specific phase may induce local changes in the lipid surface pressure, triggering the change in domain size. Experiments: To test this hypothesis, ATP synthase was incorporated into phase-separated lipid monolayers by leveraging its specific interaction with cardiolipin (CL). The ATP synthase assembly and its co-localization within CL-rich phases were characterized to assess the enzyme’s role in domain modulation. The effect of rotational forces on phase dynamics was analyzed, with particular attention to the change in size of protein-enriched and protein-devoid lipid domains. The system was characterized using fluorescence video microscopy and quantitative analysis of domain contour fluctuations. Findings: Upon ATP addition, protein-enriched domains increased in size, while protein-devoid domains contracted. The observed changes followed the 2D Young-Laplace equation, where the spinning motion of ATP synthase reduces the lateral pressure in the protein-enriched phase. The unbalanced surface pressure between phases drives the domain size modulation; which is sensitive to variations in the surface pressure difference between lipid phases as small as 10-9N/m. These findings show that ATP synthase activity can dynamically regulate lipid phase separation by modifying interfacial properties and kinetic constraints.
Fil: Carrillo Godoy, Nuria. Universidad Complutense de Madrid. Facultad de Ciencias Químicas; España
Fil: Valdivieso González, David. Universidad Complutense de Madrid. Facultad de Ciencias Químicas; España
Fil: Natale, Paolo. Universidad Complutense de Madrid. Facultad de Ciencias Químicas; España
Fil: Ritacco, Hernán Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; Argentina
Fil: Cao García, Francisco J.. Universidad Complutense de Madrid. Facultad de Ciencias Químicas; España
Fil: Almendro Vedia, Víctor G.. Universidad Complutense de Madrid. Facultad de Ciencias Químicas; España
Fil: López Montero, Iván. Universidad Complutense de Madrid. Facultad de Ciencias Químicas; España
Materia
ATP synthase
Biological Spinners
Lipid Monolayers
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/281725
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Protein nanorotors control the size of lipid domains in phase-separated monolayersCarrillo Godoy, NuriaValdivieso González, DavidNatale, PaoloRitacco, Hernán AlejandroCao García, Francisco J.Almendro Vedia, Víctor G.López Montero, IvánATP synthaseBiological SpinnersLipid Monolayershttps://purl.org/becyt/ford/1.3https://purl.org/becyt/ford/1Hypothesis: Phase separation in lipid membranes leads to the formation of distinct lipid domains, which are influenced by kinetic factors and interfacial phenomena. While line tension has been considered a key determinant of domain size, studies suggest that kinetic effects play a significant role. We hypothesize that modifying in situ the surface pressure difference between coexisting lipid phases can regulate domain size. Specifically, the rotational activity of ATP synthase embedded in a specific phase may induce local changes in the lipid surface pressure, triggering the change in domain size. Experiments: To test this hypothesis, ATP synthase was incorporated into phase-separated lipid monolayers by leveraging its specific interaction with cardiolipin (CL). The ATP synthase assembly and its co-localization within CL-rich phases were characterized to assess the enzyme’s role in domain modulation. The effect of rotational forces on phase dynamics was analyzed, with particular attention to the change in size of protein-enriched and protein-devoid lipid domains. The system was characterized using fluorescence video microscopy and quantitative analysis of domain contour fluctuations. Findings: Upon ATP addition, protein-enriched domains increased in size, while protein-devoid domains contracted. The observed changes followed the 2D Young-Laplace equation, where the spinning motion of ATP synthase reduces the lateral pressure in the protein-enriched phase. The unbalanced surface pressure between phases drives the domain size modulation; which is sensitive to variations in the surface pressure difference between lipid phases as small as 10-9N/m. These findings show that ATP synthase activity can dynamically regulate lipid phase separation by modifying interfacial properties and kinetic constraints.Fil: Carrillo Godoy, Nuria. Universidad Complutense de Madrid. Facultad de Ciencias Químicas; EspañaFil: Valdivieso González, David. Universidad Complutense de Madrid. Facultad de Ciencias Químicas; EspañaFil: Natale, Paolo. Universidad Complutense de Madrid. Facultad de Ciencias Químicas; EspañaFil: Ritacco, Hernán Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; ArgentinaFil: Cao García, Francisco J.. Universidad Complutense de Madrid. Facultad de Ciencias Químicas; EspañaFil: Almendro Vedia, Víctor G.. Universidad Complutense de Madrid. Facultad de Ciencias Químicas; EspañaFil: López Montero, Iván. Universidad Complutense de Madrid. Facultad de Ciencias Químicas; EspañaAcademic Press Inc Elsevier Science2025-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/vnd.openxmlformats-officedocument.wordprocessingml.documentapplication/pdfhttp://hdl.handle.net/11336/281725Carrillo Godoy, Nuria; Valdivieso González, David; Natale, Paolo; Ritacco, Hernán Alejandro; Cao García, Francisco J.; et al.; Protein nanorotors control the size of lipid domains in phase-separated monolayers; Academic Press Inc Elsevier Science; Journal of Colloid and Interface Science; 698; 11-2025; 1-110021-9797CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0021979725014523info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jcis.2025.138061info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2026-03-31T15:15:24Zoai:ri.conicet.gov.ar:11336/281725instacron: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:34982026-03-31 15:15:24.567CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Protein nanorotors control the size of lipid domains in phase-separated monolayers
title Protein nanorotors control the size of lipid domains in phase-separated monolayers
spellingShingle Protein nanorotors control the size of lipid domains in phase-separated monolayers
Carrillo Godoy, Nuria
ATP synthase
Biological Spinners
Lipid Monolayers
title_short Protein nanorotors control the size of lipid domains in phase-separated monolayers
title_full Protein nanorotors control the size of lipid domains in phase-separated monolayers
title_fullStr Protein nanorotors control the size of lipid domains in phase-separated monolayers
title_full_unstemmed Protein nanorotors control the size of lipid domains in phase-separated monolayers
title_sort Protein nanorotors control the size of lipid domains in phase-separated monolayers
dc.creator.none.fl_str_mv Carrillo Godoy, Nuria
Valdivieso González, David
Natale, Paolo
Ritacco, Hernán Alejandro
Cao García, Francisco J.
Almendro Vedia, Víctor G.
López Montero, Iván
author Carrillo Godoy, Nuria
author_facet Carrillo Godoy, Nuria
Valdivieso González, David
Natale, Paolo
Ritacco, Hernán Alejandro
Cao García, Francisco J.
Almendro Vedia, Víctor G.
López Montero, Iván
author_role author
author2 Valdivieso González, David
Natale, Paolo
Ritacco, Hernán Alejandro
Cao García, Francisco J.
Almendro Vedia, Víctor G.
López Montero, Iván
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv ATP synthase
Biological Spinners
Lipid Monolayers
topic ATP synthase
Biological Spinners
Lipid Monolayers
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.3
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Hypothesis: Phase separation in lipid membranes leads to the formation of distinct lipid domains, which are influenced by kinetic factors and interfacial phenomena. While line tension has been considered a key determinant of domain size, studies suggest that kinetic effects play a significant role. We hypothesize that modifying in situ the surface pressure difference between coexisting lipid phases can regulate domain size. Specifically, the rotational activity of ATP synthase embedded in a specific phase may induce local changes in the lipid surface pressure, triggering the change in domain size. Experiments: To test this hypothesis, ATP synthase was incorporated into phase-separated lipid monolayers by leveraging its specific interaction with cardiolipin (CL). The ATP synthase assembly and its co-localization within CL-rich phases were characterized to assess the enzyme’s role in domain modulation. The effect of rotational forces on phase dynamics was analyzed, with particular attention to the change in size of protein-enriched and protein-devoid lipid domains. The system was characterized using fluorescence video microscopy and quantitative analysis of domain contour fluctuations. Findings: Upon ATP addition, protein-enriched domains increased in size, while protein-devoid domains contracted. The observed changes followed the 2D Young-Laplace equation, where the spinning motion of ATP synthase reduces the lateral pressure in the protein-enriched phase. The unbalanced surface pressure between phases drives the domain size modulation; which is sensitive to variations in the surface pressure difference between lipid phases as small as 10-9N/m. These findings show that ATP synthase activity can dynamically regulate lipid phase separation by modifying interfacial properties and kinetic constraints.
Fil: Carrillo Godoy, Nuria. Universidad Complutense de Madrid. Facultad de Ciencias Químicas; España
Fil: Valdivieso González, David. Universidad Complutense de Madrid. Facultad de Ciencias Químicas; España
Fil: Natale, Paolo. Universidad Complutense de Madrid. Facultad de Ciencias Químicas; España
Fil: Ritacco, Hernán Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Física del Sur. Universidad Nacional del Sur. Departamento de Física. Instituto de Física del Sur; Argentina
Fil: Cao García, Francisco J.. Universidad Complutense de Madrid. Facultad de Ciencias Químicas; España
Fil: Almendro Vedia, Víctor G.. Universidad Complutense de Madrid. Facultad de Ciencias Químicas; España
Fil: López Montero, Iván. Universidad Complutense de Madrid. Facultad de Ciencias Químicas; España
description Hypothesis: Phase separation in lipid membranes leads to the formation of distinct lipid domains, which are influenced by kinetic factors and interfacial phenomena. While line tension has been considered a key determinant of domain size, studies suggest that kinetic effects play a significant role. We hypothesize that modifying in situ the surface pressure difference between coexisting lipid phases can regulate domain size. Specifically, the rotational activity of ATP synthase embedded in a specific phase may induce local changes in the lipid surface pressure, triggering the change in domain size. Experiments: To test this hypothesis, ATP synthase was incorporated into phase-separated lipid monolayers by leveraging its specific interaction with cardiolipin (CL). The ATP synthase assembly and its co-localization within CL-rich phases were characterized to assess the enzyme’s role in domain modulation. The effect of rotational forces on phase dynamics was analyzed, with particular attention to the change in size of protein-enriched and protein-devoid lipid domains. The system was characterized using fluorescence video microscopy and quantitative analysis of domain contour fluctuations. Findings: Upon ATP addition, protein-enriched domains increased in size, while protein-devoid domains contracted. The observed changes followed the 2D Young-Laplace equation, where the spinning motion of ATP synthase reduces the lateral pressure in the protein-enriched phase. The unbalanced surface pressure between phases drives the domain size modulation; which is sensitive to variations in the surface pressure difference between lipid phases as small as 10-9N/m. These findings show that ATP synthase activity can dynamically regulate lipid phase separation by modifying interfacial properties and kinetic constraints.
publishDate 2025
dc.date.none.fl_str_mv 2025-11
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/11336/281725
Carrillo Godoy, Nuria; Valdivieso González, David; Natale, Paolo; Ritacco, Hernán Alejandro; Cao García, Francisco J.; et al.; Protein nanorotors control the size of lipid domains in phase-separated monolayers; Academic Press Inc Elsevier Science; Journal of Colloid and Interface Science; 698; 11-2025; 1-11
0021-9797
CONICET Digital
CONICET
url http://hdl.handle.net/11336/281725
identifier_str_mv Carrillo Godoy, Nuria; Valdivieso González, David; Natale, Paolo; Ritacco, Hernán Alejandro; Cao García, Francisco J.; et al.; Protein nanorotors control the size of lipid domains in phase-separated monolayers; Academic Press Inc Elsevier Science; Journal of Colloid and Interface Science; 698; 11-2025; 1-11
0021-9797
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://linkinghub.elsevier.com/retrieve/pii/S0021979725014523
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jcis.2025.138061
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/vnd.openxmlformats-officedocument.wordprocessingml.document
application/pdf
dc.publisher.none.fl_str_mv Academic Press Inc Elsevier Science
publisher.none.fl_str_mv Academic Press Inc 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 12.822162

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