Details

Autor(en) / Beteiligte

• Silvius, John R
• Zuckermann, Martin J

Titel

Interbilayer transfer of phospholipid-anchored macromolecules via monomer diffusion

Ist Teil von

• Biochemistry (Easton), 1993-03, Vol.32 (12), p.3153-3161

Ort / Verlag

Washington, DC: American Chemical Society

Erscheinungsjahr

1993

Quelle

MEDLINE

Beschreibungen/Notizen

• A series of conjugates has been prepared by linking various hydrophilic macromolecules [poly-(ethylene glycols), polylysine, aminodextrans, or apotransferrin] to synthetic phosphatidylethanolamines via linker moieties incorporating a fluorescent bimane group. Using a fluorescence energy transfer-based assay, the rate of transfer of these species between phospholipid vesicles has been monitored as a function of the nature and size of the coupled macromolecule and of the acyl chain composition of the lipid anchor. Conjugates in which the phospholipid anchor is linked to a small hydrophilic terminal residue (e.g., ethanolamine or ethylenediamine) transfer between large unilamellar vesicles of egg phosphatidylcholine with half-times ranging from tens of minutes (for dimyristoyl lipid conjugates) to a few tens of hours (for dipalmitoyl and 1-palmitoyl-2-oleoyl lipid conjugates), in agreement with previous results for unlabeled phospholipids. Conjugation of these same lipid anchors to larger hydrophilic molecules markedly accelerates their rates of intermembrane transfer, by factors ranging from 5-7-fold (for conjugates with apotransferrin and aminodextrans of molecular weight 10,000-70,000) to over 25-fold [for conjugates with poly(ethylene glycol)-5000]. In all cases the observed transfer appears to reflect the diffusion of lipid monomers through the aqueous phase. Our results suggest that substantial intermembrane transfer can occur, on a time scale of several hours or less, for hydrophilic macromolecules conjugated to diacyl(/alkyl) lipids with 14- to 18-carbon chains unless portions of the conjugate other than the lipid anchor also interact strongly with the membrane.