ELECTROPHORETIC AND DYNAMIC LIGHT-SCATTERING STUDY OF THE INTERACTIONOF CYTOCHROME-C WITH DIMYRISTOYL PHOSPHATIDYLGLYCEROL, DIMYRISTOYLPHOSPHATIDYLCHOLINE, AND INTRAMEMBRANOUSLY MIXED LIPOSOMES
B. Demeulenaer et al., ELECTROPHORETIC AND DYNAMIC LIGHT-SCATTERING STUDY OF THE INTERACTIONOF CYTOCHROME-C WITH DIMYRISTOYL PHOSPHATIDYLGLYCEROL, DIMYRISTOYLPHOSPHATIDYLCHOLINE, AND INTRAMEMBRANOUSLY MIXED LIPOSOMES, Journal of colloid and interface science, 189(2), 1997, pp. 254-258
The binding of cytochrome c to liposomes was studied by electrophoreti
c light scattering and dynamic light scattering measurements. Pure dim
yristoylphosphatidylglycerol (DMPG) and dimyristoylphosphatidylcholine
(DMPC), as well as intramembranously mixed DMPC-DMPG liposomal disper
sions were investigated, Thus, the charge density of the liposomes was
varied within a broad range, Because of adsorption of the protein ont
o the anionic liposome types, the electrophoretic mobility of the DMPG
-containing liposomal dispersions was significantly reduced, These res
ults confirmed the generally accepted model of interaction between cyt
ochrome c and phospholipids, which assumes the adsorption process to b
e electrostatically controlled; however, the experimentally observed c
harge reinversion phenomenon indicated that some other type(s) of inte
raction(s) between phospholipids and cytochrome c seems to control the
overall binding process as well. From dynamic light scattering measur
ements it was found that cytochrome c addition induced DMPG liposome a
ggregation, From the dependence of the aggregation kinetics on the cyt
ochrome c-to-phospholipid ratio, it was deduced that charge neutraliza
tion was accompanied by bridging, especially at lower protein-to-DMPG
ratios. (C) 1997 Academic Press.