Modification of phospholipid structure results in greater stability if liposomes in serum.

Previous studies have revealed that the replacement of the C-2 ester group in phosphatidylcholine by the carbamyloxy function renders the resulting lipids, without affecting the properties of the liposomes, resistant to hydrolysis by phospholipase A2 (Gupta, C.M. Bali, A. (1981) Biochim. Biophys, Acta 663, 506-515). As an extension of this work, the effect of serum on the stability of liposomes, prepared from 1-palmitoyl-2-heptadec-10-cis-enylcarbamyloxyphosphatidylcholine (carbamylphosphatidylcholine), has been examined. The stability has been measured in terms of (a) bilayer permeability to solutes, and (b) the lipid transfer to serum proteins. Replacement of egg phosphatidylcholine in liposomes by the carbamyl analog prevented serum-induced leakage of the entrapped solutes and also inhibited the lipid (phospholipid and cholesterol) transfer. Manipulation of the cholesterol content of the liposomes had no effect on the stability. These observations indicate that the interaction of serum proteins with liposomes probably involves a highly specific binding of the proteins to the liposome surface.