The lateral diffusion of selectively aggregated peptides in giant unilamellar vesicles

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DOIResolve DOI: http://doi.org/10.1016/S0006-3495(03)74983-2
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TypeArticle
Journal titleBiophysical Journal
Volume84
Issue3
Pages17561764; # of pages: 9
AbstractWe have systematically investigated the effect of aggregation of a transmembrane peptide on its diffusion in dimyristoylphosphatidylcholine and in palmitoyloleoylphosphatidylcholine model membranes. The hydrophobic segment of the b subunit from E. coli F₁F₀-ATP synthase was modified with a histidine tag at the carbonyl terminus and was aggregated selectively by using a series of multivalent, dendritic chelating agents with nitrilotriacetic acid functional groups. Peptide complexes ranging from monomers to hexamers were formed and studied in giant unilamellar vesicles. The rate of diffusion for the transmembrane peptide complexes were found to depend on the size of the complex. The results agree with predictions from the free area model for monomers and dimers, and the hydrodynamic continuum model for tetramers, pentamers, and hexamers. Comparisons with diffusion of lipids confirm that the diffusion of a transmembrane peptide is enhanced by coupling of density fluctuations between the two monolayers.
Publication date
PublisherElsevier for the Biophysical Society
LanguageEnglish
Peer reviewedYes
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NPARC number12328463
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Record identifiercaec2370-b33a-4939-86dd-1db5960438f3
Record created2009-09-10
Record modified2017-07-25
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