Membrane lipid phase behaviour and lipid-protein interactions

1990 ◽  
Vol 18 (2) ◽  
pp. 133-136 ◽  
Author(s):  
P. J. QUINN
Keyword(s):  
Protein Interactions ◽  
Membrane Lipid ◽  
Phase Behaviour ◽  
Lipid Phase ◽  
Lipid Protein Interactions

Membrane Lipid-Protein Interactions

2017 ◽  
pp. 61-84 ◽  
Author(s):  
Michael F. Brown ◽  
Udeep Chawla ◽  
Suchithranga M. D. C. Perera
Keyword(s):  
Protein Interactions ◽  
Membrane Lipid ◽  
Lipid Protein Interactions

Cold-induced lipid phase transitions

1990 ◽  
Vol 326 (1237) ◽  
pp. 555-570 ◽  
Keyword(s):  
Low Temperatures ◽  
Membrane Lipids ◽  
Weak Interactions ◽  
Protective Action ◽  
Biological Membranes ◽  
Membrane Lipid ◽  
Phase Behaviour ◽  
Lipid Phase ◽  
Aqueous Environment ◽  
Factors Affecting

The structural organization of biological membranes is largely determined by the weak interactions existing between their components and between these components and their aqueous environment. These interactions are particularly sensitive to changes in temperature and hydration. The factors influencing membrane lipid phase behaviour are briefly reviewed and used to develop a phase-separation model describing the response of biological membranes to stress. The factors affecting the interaction of cryoprotectants with membrane lipids are explored and their role in the stabilization of membrane organization at low temperatures discussed. It is suggested that the basis of their protective action lies in an ability to preserve the balance of interactions between membrane components at low temperatures at a level similar to that existing under physiological conditions.

scholarly journals Model Membrane Systems Used to Study Plasma Membrane Lipid Asymmetry

Symmetry ◽  
2021 ◽  
Vol 13 (8) ◽  
pp. 1356
Author(s):  
Haden L. Scott ◽  
Kristen B. Kennison ◽  
Thais A. Enoki ◽  
Milka Doktorova ◽  
Jacob J. Kinnun ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Plasma Membranes ◽  
Membrane Lipid ◽  
Model Membrane ◽  
Model Membranes ◽  
Computational Techniques ◽  
Symmetric Model ◽  
Membrane Asymmetry ◽  
Asymmetric Model ◽  
Lipid Protein Interactions

It is well known that the lipid distribution in the bilayer leaflets of mammalian plasma membranes (PMs) is not symmetric. Despite this, model membrane studies have largely relied on chemically symmetric model membranes for the study of lipid–lipid and lipid–protein interactions. This is primarily due to the difficulty in preparing stable, asymmetric model membranes that are amenable to biophysical studies. However, in the last 20 years, efforts have been made in producing more biologically faithful model membranes. Here, we review several recently developed experimental and computational techniques for the robust generation of asymmetric model membranes and highlight a new and particularly promising technique to study membrane asymmetry.

Reconstitution of lipoproteins. II. Lipid–protein interaction between dimyristoyl-lecithin and dimyristoyl-lecithin:cholesterol vesicles and purified apolipoprotein C-I and C-III2 studied by isomeric spin-labelled lecithins

1980 ◽  
Vol 58 (7) ◽  
pp. 592-598 ◽  
Author(s):  
D. J. Vaughan ◽  
W. C. Breckenridge ◽  
N. Z. Stanacev
Keyword(s):  
Protein Interactions ◽  
Phase Changes ◽  
Phospholipid Bilayer ◽  
Head Group ◽  
Lipid Phase ◽  
Resonance Spectroscopy ◽  
Apolipoprotein C ◽  
Lipid Protein Interaction ◽  
Lipid Protein Interactions ◽  
Induced Changes

The reconstitution of purified apolipoprotein C-I and C-III2 with sn-3-dimyristoyl-lecithin and sn-3-dimyristoyl-lecithin:cholesterol (10:1) vesicles was studied by electron spin resonance spectroscopy using isomeric 5′-, 12′-, and 16′-(N-oxyl-4″,4″-dimethyloxazolidine)stearoyl spin-labelled lecithin probes. Results obtained from the temperature-induced changes of lipoprotein recombinants showed the hydrophilic nature of the lipid–protein interactions. The temperature-induced phospholipid phase transition, as measured by 5′-(N-oxyl-4″,4″-dimethyloxazolidine)stearoyl spin-labelled lecithin probe in recombinants containing apoprotein C-1 or apoprotein C-III2, is very broad and has a small cooperative unit indicative of extensive lipid–protein interactions occurring at the head group region of the phospholipid bilayer. When 12′- and 16′-(N-oxyl-4″,4″-dimethyloxazolidine)stearoyl spin-labelled lecithins are used as probes in the same system, similar sharper and more cooperative lipid phase changes are detected. These results indicate a surface location for both apoprotein C-I and apoprotein C-III2 with respect to the phospholipid bilayer in lipoprotein recombinants with and without cholesterol.

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