scholarly journals Interaction of soluble and membrane proteins with monolayers of glycosphingolipids

1982 ◽  
Vol 203 (3) ◽  
pp. 717-725 ◽  
Author(s):  
G D Fidelio ◽  
B Maggio ◽  
F A Cumar
Keyword(s):  
Membrane Proteins ◽  
Surface Potential ◽  
Protein Interactions ◽  
Lipid Monolayers ◽  
Anionic Phospholipids ◽  
Surface Potential Measurements ◽  
Lipid Protein Interaction ◽  
Lipid Protein Interactions ◽  
The Individual ◽  
Free Interfaces

1. The interactions of four proteins (albumin, myelin basic protein, melittin and glycophorin) with eight neutral or acidic glycosphingolipids, including sulphatides and gangliosides, five zwitterionic or anionic phospholipids and some of their mixtures, were studied in lipid monolayers at the air/145 mM-NaCl interface. 2. In lipid-free interfaces, the surface pressure and surface potential reached by either soluble or integral membrane proteins did not reveal marked differences. 3. All the proteins studied showed interactions with each of the lipids but the maximal interactions were found for basic proteins with acidic glycosphingolipids. 4. Surface-potential measurements indicated that different dipolar organizations at the interface can be adopted by lipid-protein interactions showing the same value for surface free energy. 5. The individual surface properties of either the lipid of protein component are modified as a consequence of the lipid-protein interaction. 6. In mixed-lipid monolayers, the composition of the interface may affect the lipid-protein interactions in a non-proportional manner with respect to the relative amount of the individual lipid components.

scholarly journals Lipid-protein interactions are unique fingerprints for membrane proteins

2017 ◽  
Author(s):  
Valentina Corradi ◽  
Eduardo Mendez-Villuendas ◽  
Helgi I. Ingólfsson ◽  
Ruo-Xu Gu ◽  
Iwona Siuda ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Protein Interactions ◽  
Cell Membranes ◽  
Spatiotemporal Resolution ◽  
Lipid Dynamics ◽  
Lipid Species ◽  
Lipid Environment ◽  
Lipid Protein Interactions ◽  
Dynamics Simulations ◽  
Asymmetrically Distributed

ABSTRACTCell membranes contain hundreds of different proteins and lipids in an asymmetric arrangement. Understanding the lateral organization principles of these complex mixtures is essential for life and health. However, our current understanding of the detailed organization of cell membranes remains rather elusive, owing to the lack of experimental methods suitable for studying these fluctuating nanoscale assemblies of lipids and proteins with the required spatiotemporal resolution. Here, we use molecular dynamics simulations to characterize the lipid environment of ten membrane proteins. To provide a realistic lipid environment, the proteins are embedded in a model plasma membrane, where more than 60 lipid species are represented, asymmetrically distributed between leaflets. The simulations detail how each protein modulates its local lipid environment through local lipid composition, thickness, curvature and lipid dynamics. Our results provide a molecular glimpse of the complexity of lipid-protein interactions, with potentially far reaching implications for the overall organization of the cell membrane.

scholarly journals Lipid-Protein Interactions of Integral Membrane Proteins: A Comparative Simulation Study

2004 ◽  
Vol 87 (6) ◽  
pp. 3737-3749 ◽  
Author(s):  
Sundeep S. Deol ◽  
Peter J. Bond ◽  
Carmen Domene ◽  
Mark S.P. Sansom
Keyword(s):  
Membrane Proteins ◽  
Protein Interactions ◽  
Simulation Study ◽  
Integral Membrane Proteins ◽  
Lipid Protein Interactions

scholarly journals Lipid–Protein Interactions Are Unique Fingerprints for Membrane Proteins

2018 ◽  
Vol 4 (6) ◽  
pp. 709-717 ◽  
Author(s):  
Valentina Corradi ◽  
Eduardo Mendez-Villuendas ◽  
Helgi I. Ingólfsson ◽  
Ruo-Xu Gu ◽  
Iwona Siuda ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Protein Interactions ◽  
Lipid Protein Interactions

Molecular simulations and lipid–protein interactions: potassium channels and other membrane proteins

2005 ◽  
Vol 33 (5) ◽  
pp. 916-920 ◽  
Author(s):  
M.S.P. Sansom ◽  
P.J. Bond ◽  
S.S. Deol ◽  
A. Grottesi ◽  
S. Haider ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Binding Site ◽  
Protein Interactions ◽  
Outer Membrane Proteins ◽  
Lipid Binding ◽  
Potassium Channel Kcsa ◽  
Head Groups ◽  
Arginine Residues ◽  
Lipid Protein Interactions ◽  
Dynamics Simulations

Molecular dynamics simulations may be used to probe the interactions of membrane proteins with lipids and with detergents at atomic resolution. Examples of such simulations for ion channels and for bacterial outer membrane proteins are described. Comparison of simulations of KcsA (an α-helical bundle) and OmpA (a β-barrel) reveals the importance of two classes of side chains in stabilizing interactions with the head groups of lipid molecules: (i) tryptophan and tyrosine; and (ii) arginine and lysine. Arginine residues interacting with lipid phosphate groups play an important role in stabilizing the voltage-sensor domain of the KvAP channel within a bilayer. Simulations of the bacterial potassium channel KcsA reveal specific interactions of phosphatidylglycerol with an acidic lipid-binding site at the interface between adjacent protein monomers. A combination of molecular modelling and simulation reveals a potential phosphatidylinositol 4,5-bisphosphate-binding site on the surface of Kir6.2.

scholarly journals Assessing the Role of Lipids in the Molecular Mechanism of Membrane Proteins

2021 ◽  
Vol 22 (14) ◽  
pp. 7267
Author(s):  
Léni Jodaitis ◽  
Thomas van Oene ◽  
Chloé Martens
Keyword(s):  
Membrane Proteins ◽  
Molecular Mechanism ◽  
Protein Interactions ◽  
Protein Function ◽  
Biological Membrane ◽  
Allosteric Coupling ◽  
Lipid Protein Interactions ◽  
Experimental Challenge ◽  
Membrane Protein Function

Membrane proteins have evolved to work optimally within the complex environment of the biological membrane. Consequently, interactions with surrounding lipids are part of their molecular mechanism. Yet, the identification of lipid–protein interactions and the assessment of their molecular role is an experimental challenge. Recently, biophysical approaches have emerged that are compatible with the study of membrane proteins in an environment closer to the biological membrane. These novel approaches revealed specific mechanisms of regulation of membrane protein function. Lipids have been shown to play a role in oligomerization, conformational transitions or allosteric coupling. In this review, we summarize the recent biophysical approaches, or combination thereof, that allow to decipher the role of lipid–protein interactions in the mechanism of membrane proteins.

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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