Interaction of recombinant human interferon-gamma with liposomes.
The interaction of recombinant human interferon-gamma (IFN) with egg phosphatidylcholine liposomes was studied. IFN which binds to liposomes was dependent on the liposomal charge and pH, and a preferential binding was observed in negatively charged liposomes at pH 7.4-10. Electron-microscopic observation showed that the increased liposomal turbidity induced by IFN was due to liposomal aggregation, and the increased turbidity could be decreased by the addition of NaCl. Thus, ionic binding may participate in this interaction. But, when the incubation time was longer, the liposomal aggregation was not decreased by the addition of NaCl, and the leakage of the entrapped marker, calcein, was observed. Electron-microscopic analysis showed that this leakage resulted from the morphological change of liposomes. From these findings, ionic binding may participate in the interaction between IFN and liposomes and then develop a morphological change in negatively charged liposomes under the neutral pH condition.
Ishihara
H
H
Tokyo College of Pharmacy, Japan.
Hara
T
T
Aramaki
Y
Y
Tsuchiya
S
S
Hosoi
K
K
D005452:Fluoresceins / Q000737:chemistry; D006801:Humans; D007371:Interferon-gamma / Q000737:chemistry*; D008081:Liposomes / Q000737:chemistry*; D009391:Nephelometry and Turbidimetry; D011994:Recombinant Proteins; D013050:Spectrometry, Fluorescence
D005452:Fluoresceins; D008081:Liposomes; D011994:Recombinant Proteins; D007371:Interferon-gamma; C007740:fluorexon