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The Lateral Diffusion of Selectively Aggregated Peptides in Giant Unilamellar Vesicles

Department of Chemistry, The University of Western Ontario, London, Ontario N6A 5B7, Canada

Correspondence: Address reprint requests to Nils O. Petersen, Dept. of Chemistry, The University of Western Ontario, London, ON N6A 5B7, Canada. Tel.: 519-661-3812; Fax: 519-661-3139; E-mail: petersen{at}uwo.ca.

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.

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