Electrophoretic and dynamic light scattering study of the interaction of cytochrome c with dimyristoyl phosphatidylglycerol, dimyristoylphosphatidylcholine, and intramembranously mixed liposomes

被引:12
作者
DeMeulenaer, B
VanderMeeren, P
DeCuyper, M
Vanderdeelen, J
Baert, L
机构
[1] STATE UNIV GHENT,FAC AGR & APPL BIOL SCI,DEPT APPL ANALYT & PHYS CHEM,B-9000 GHENT,BELGIUM
[2] KATHOLIEKE UNIV LEUVEN,INTERDISCIPLINARY RES CTR,B-8500 KORTRIJK,BELGIUM
关键词
cytochrome c; dimyristoylphosphatidylglycerol; dimyristoylphosphatidylcholine; liposomes; dynamic light scattering; electrophoretic light scattering; PROTEIN INTERACTIONS; BINDING; MEMBRANES;
D O I
10.1006/jcis.1997.4789
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
The binding of cytochrome c to liposomes was studied by electrophoretic light scattering and dynamic light scattering measurements. Pure dimyristoylphosphatidylglycerol (DMPG) and dimyristoylphosphatidylcholine (DMPC), as well as intramembranously mixed DMPC-DMPG liposomal dispersions were investigated, Thus, the charge density of the liposomes was varied within a broad range, Because of adsorption of the protein onto the anionic liposome types, the electrophoretic mobility of the DMPG-containing liposomal dispersions was significantly reduced, These results confirmed the generally accepted model of interaction between cytochrome c and phospholipids, which assumes the adsorption process to be electrostatically controlled; however, the experimentally observed charge reinversion phenomenon indicated that some other type(s) of interaction(s) between phospholipids and cytochrome c seems to control the overall binding process as well. From dynamic light scattering measurements it was found that cytochrome c addition induced DMPG liposome aggregation, From the dependence of the aggregation kinetics on the cytochrome c-to-phospholipid ratio, it was deduced that charge neutralization was accompanied by bridging, especially at lower protein-to-DMPG ratios. (C) 1997 Academic Press.
引用
收藏
页码:254 / 258
页数:5
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