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Título

Modeling the interplay between protein and lipid aggregation in supported membranes

AutorGonzález de Prado Salas, Pablo; Encinar, Mario ; Alonso Caballero, Álvaro ; Vélez, Marisela ; Tarazona, Pedro
Palabras claveTheoretical model
Dynamic protein filaments
Supported bilayers
Protein–lipid interactions
Atomic force microscopy
Lipid domains
Fecha de publicaciónene-2015
EditorElsevier
CitaciónChemistry and Physics of Lipids 185: 141-152 (2015)
Resumen© 2014 Elsevier Ireland Ltd. All rights reserved. We present a theoretical model that deals with the complex interplay between lipid segregation and the self-aggregation of lipid-attached proteins. The model, in contrast to previous ones that consider proteins only as passive elements affecting the lipid distribution, describes the system including three terms: the dynamic interactions between protein monomers, the interactions between lipid components, and a mixed term considering protein-lipid interactions. It is used to explain experimental results performed on a well-defined system in which a self-aggregating soluble bacterial cytoskeletal protein polymerizes on a lipid bilayer containing two lipid components. All the elements considered in a previously described protein model, including torsion of the monomers within the filament, are needed to account for the observed filament shapes. The model also points out that lipid segregation can affect the length and curvature of the filaments and that the dynamic behavior of the lipids and proteins can have different time scales, giving rise to memory effects. This simple model that considers a dynamic protein assembly on a fluid and active lipid surface can be easily extended to other biologically relevant situations in which the interplay between protein and lipid aggregation is needed to fully describe the system.
Versión del editorhttp://dx.doi.org/10.1016/j.chemphyslip.2014.06.006
URIhttp://hdl.handle.net/10261/118303
DOI10.1016/j.chemphyslip.2014.06.006
Identificadoresdoi: 10.1016/j.chemphyslip.2014.06.006
issn: 1873-2941
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