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Macromolecular Crowding at Membrane Interfaces: Adsorption and Alignment of Membrane Peptides
Umeå University, Faculty of Science and Technology, Chemistry.
Umeå University, Faculty of Science and Technology, Chemistry.
2008 (English)In: Journal of Molecular Biology, ISSN 1089-8638, Vol. 375, 376-85 p.Article in journal (Refereed) Published
Abstract [en]

Association of proteins to cellular membranes is involved in various biological processes. Various theoretical models have been developed to describe this adsorption mechanism, commonly implying the concept of an ideal solution. However, due to the two-dimensional character of membrane surfaces intermolecular interactions between the adsorbed molecules become important. Therefore previously adsorbed molecules can influence the adsorption behavior of additional protein molecules and their membrane-associated structure. Using the model peptide LAH4, which upon membrane-adsorption can adopt a transmembrane as well as an in-planar configuration, we carried out a systematic study of the correlation between the peptide concentration in the membrane and the topology of this membrane-associated polypeptide. We could describe the observed binding behavior by establishing a concept, which includes intermolecular interactions in terms of a scaled particle theory.

High surface concentration of the peptide shifts the molecules from an in-planar into a transmembrane conformation, a process driven by the reduction of occupied surface area per molecule. In a cellular context, the crowding-dependent alignment might provide a molecular switch for a cell to sense and control its membrane occupancy. Furthermore, crowding might have pronounced effects on biological events, such as the cooperative behavior of antimicrobial peptides and the membrane triggered aggregation of amyloidogenic peptides.

Place, publisher, year, edition, pages
2008. Vol. 375, 376-85 p.
Keyword [en]
peptide-lipid interactions, macromolecular crowding, lipid membranes, surface crowding, antibiotic peptides
Identifiers
URN: urn:nbn:se:umu:diva-6126DOI: doi:10.1016/j.jmb.2007.10.053PubMedID: 18022193OAI: oai:DiVA.org:umu-6126DiVA: diva2:145794
Available from: 2007-12-07 Created: 2007-12-07 Last updated: 2011-01-10Bibliographically approved

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