L. Fleury et al., PREPARATION AND CHARACTERIZATION OF DIPALMITOYLPHOSPHATIDYLCHOLINE LIPOSOMES CONTAINING INTERLEUKIN-2, Brazilian journal of medical and biological research, 28(5), 1995, pp. 519-529
Human recombinant interleukin-2 (IL-2) has been associated or mixed wi
th small unilamellar vesicles prepared from dipalmitoylphosphatidylcho
line (DPPC). Whatever the mode of IL-2 introduction, a considerable pr
oportion of the added protein was associated with the liposomes, as de
termined by gel filtration and ultrafiltration/centrifugation, suggest
ing that IL-2 can interact with the lipid bilayer as well as being ent
rapped within the aqueous phase. Moreover, IL-2 prevented the aggregat
ion/fusion of the vesicles at 4 degrees C. Liposome-associated protein
was partially protected from digestion by pepsin, especially at the C
-terminal, since no fluorescence emission from the tryptophan in this
region was detected in the resulting peptides after separation by HPLC
. Such systems could constitute a sustained release form of IL-2 for i
mmunotherapy.