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The lateral diffusion of selectively aggregated peptides in giant unilamellar vesicles

From National Research Council Canada

DOIResolve DOI: https://doi.org/10.1016/S0006-3495(03)74983-2
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FormatText, Article
Abstract
We 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
In
  • Biophysical Journal 84, no. 3: 1756–1764.
LanguageEnglish
Peer reviewedYes
NRC publication
This is a non-NRC publication

"Non-NRC publications" are publications authored by NRC employees prior to their employment by NRC.

NPARC number12328463
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Record identifiercaec2370-b33a-4939-86dd-1db5960438f3
Record created2009-09-10
Record modified2020-04-02
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