RT Journal Article
T1 Protein nanorotors control the size of lipid domains in phase-separated monolayers
A1 Carrillo Godoy, Nuria
A1 Valdivieso González, David
A1 Natale, Paolo
A1 Ritacco, Hernán
A1 Cao García, Francisco Javier
A1 Almendro Vedia, Víctor Galileo
A1 López Montero, Iván
AB 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.
PB Elsevier
SN 0021-9797
YR 2025
FD 2025
LK https://hdl.handle.net/20.500.14352/121522
UL https://hdl.handle.net/20.500.14352/121522
LA eng
NO Nuria Carrillo-Godoy, David Valdivieso González, Paolo Natale, Hernán Ritacco, Francisco J. Cao-García, Víctor G. Almendro-Vedia, Iván López-Montero, Protein nanorotors control the size of lipid domains in phase-separated monolayers, Journal of Colloid and Interface Science, Volume 698, 2025, 138061, https://doi.org/10.1016/j.jcis.2025.138061.
NO Authorship contribution statement:Nuria Carrillo-Godoy: Writing – review & editing, Investigation, Data curation. David Valdivieso González: Writing – review & editing, Investigation. Paolo Natale: Writing – review & editing, Resources, Methodology. Hernán Ritacco: Writing – review & editing, Writing – original draft, Investigation, Data curation. Francisco J. Cao-García: Writing – original draft, Formal analysis. Víctor G. Almendro-Vedia: Writing – review & editing, Supervision, Data curation. Iván López-Montero: Writing – review & editing, Writing – original draft, Supervision, Funding acquisition, Conceptualization.
NO Ministerio de Ciencia, Innovación y Universidades (España)
NO Universidad Complutense de Madrid
NO Banco Santander
NO Agencia Nacional de Promoción de la Investigación, el Desarrollo Tecnológico y la Innovación (Argentina)
NO Consejo Nacional de Investigaciones Científicas y Técnicas (Argentina)
NO Universidad Nacional del Sur (Argentina)
DS Docta Complutense
RD 23 dic 2025