Formation and dissolution of phospholipid domains with varying textures in hybrid lipo-polymersomes

Soft Matter ◽  
2012 ◽  
Vol 8 (30) ◽  
pp. 7982 ◽  
Author(s):  
Jin Nam ◽  
T. Kyle Vanderlick ◽  
Paul A. Beales
Keyword(s):  
2009 ◽  
Vol 30 (2) ◽  
Author(s):  
I. Solomonov ◽  
J. Daillant ◽  
G. Fragneto ◽  
K. Kjaer ◽  
J. S. Micha ◽  
...  

1986 ◽  
Vol 56 (24) ◽  
pp. 2633-2636 ◽  
Author(s):  
A. Miller ◽  
W. Knoll ◽  
H. Möhwald

Biochemistry ◽  
1991 ◽  
Vol 30 (20) ◽  
pp. 4909-4916 ◽  
Author(s):  
R. Tampe ◽  
A. Von Lukas ◽  
H. J. Galla
Keyword(s):  

2010 ◽  
Vol 1798 (5) ◽  
pp. 1014-1019 ◽  
Author(s):  
Laura Picas ◽  
Adrián Carretero-Genevrier ◽  
M. Teresa Montero ◽  
J.L. Vázquez-Ibar ◽  
Bastien Seantier ◽  
...  

1987 ◽  
Vol 91 (25) ◽  
pp. 6417-6422 ◽  
Author(s):  
D. J. Keller ◽  
J. P. Korb ◽  
H. M. McConnell

2000 ◽  
Vol 182 (4) ◽  
pp. 1172-1175 ◽  
Author(s):  
Eugenia Mileykovskaya ◽  
William Dowhan

ABSTRACT Cardiolipin (CL)-specific fluorescent dye 10-N-nonyl-acridine orange (NAO) was used to visualize CL distribution in Escherichia coli cells of different phospholipid compositions. In a filamentous mutant containing only anionic phospholipids, green fluorescent spots were observed along the filaments at approximately regular intervals. Three-dimensional image reconstruction obtained by optical sectioning and a deconvolution algorithm revealed NAO-binding domains in the plane of the cell membrane. Substantial red fluorescence emission of bound NAO supported labeling of CL-containing domains. These structures were not found in mutants deficient in CL biosynthesis. The domains were also observed mostly in the septal region and on the poles in cells of normal size with wild-type phospholipid composition.


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