scholarly journals Glucose-Based Fluorinated Surfactants as Additives for the Crystallization of Membrane Proteins: Synthesis and Preliminary Physical–Chemical and Biochemical Characterization

ACS Omega ◽  
2021 ◽  
Author(s):  
Moheddine Wehbie ◽  
Ilham Bouchemal ◽  
Anaïs Deletraz ◽  
Eva Pebay-Peyroula ◽  
Cécile Breyton ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Biochemical Characterization ◽  
Fluorinated Surfactants ◽  
Physical Chemical

Free-Standing Films of Fluorinated Surfactants as 2D Matrices for Organizing Detergent-Solubilized Membrane Proteins

Langmuir ◽  
2007 ◽  
Vol 23 (8) ◽  
pp. 4303-4309 ◽  
Author(s):  
Vera Petkova ◽  
Jean-Jacques Benattar ◽  
Manuela Zoonens ◽  
Francesca Zito ◽  
Jean-Luc Popot ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Free Standing ◽  
Fluorinated Surfactants

Lactobionamide Surfactants with Hydrogenated, Perfluorinated or Hemifluorinated Tails:  Physical-Chemical and Biochemical Characterization

Langmuir ◽  
2006 ◽  
Vol 22 (21) ◽  
pp. 8881-8890 ◽  
Author(s):  
Florence Lebaupain ◽  
Andrés G. Salvay ◽  
Blandine Olivier ◽  
Grégory Durand ◽  
Anne-Sylvie Fabiano ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Physical Chemical

Biochemical Characterization, Structure and Transport of Lysosomal Integral Membrane Proteins

Endocytosis ◽  
1992 ◽  
pp. 213-220
Author(s):  
B. Seguí-Real ◽  
M. A. Vega ◽  
J. G. Barriocanal ◽  
L. Yuan ◽  
J. Alcalde ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Biochemical Characterization ◽  
Integral Membrane Proteins

scholarly journals Functional reassembly of membrane proteins in planar lipid bilayers

1981 ◽  
Vol 14 (1) ◽  
pp. 1-79 ◽  
Author(s):  
M. Montal ◽  
A. Darszon ◽  
H. Schindler
Keyword(s):  
Membrane Proteins ◽  
Lipid Bilayers ◽  
Recent Progress ◽  
Molecular Mechanisms ◽  
Biochemical Characterization ◽  
Structural Information ◽  
Energy Transduction ◽  
Biological Processes ◽  
Membrane Biology ◽  
Technical Advances

Recent progress in membrane biology has brought us to a stage where it is possible to associate complex biological processes to identifiable membrane proteins. Technical advances in the biochemical characterization and purification of membrane proteins have contributed a wealth of structural information. The reconstitution approach has proved to be valuable in our efforts to understand the molecular mechanisms of membrane transport and energy transduction.

scholarly journals Fluorinated and hemifluorinated surfactants as alternatives to detergents for membrane protein cell-free synthesis

2007 ◽  
Vol 403 (1) ◽  
pp. 183-187 ◽  
Author(s):  
Kyu-Ho Park ◽  
Catherine Berrier ◽  
Florence Lebaupain ◽  
Bernard Pucci ◽  
Jean-Luc Popot ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Lipid Vesicles ◽  
Mechanosensitive Channel ◽  
In Vitro Synthesis ◽  
Fluorinated Surfactants ◽  
Electrophysiological Activity ◽  
Protein Cell ◽  
Suitable Environment

Hemifluorinated and fluorinated surfactants are lipophobic and, as such, non-detergent. Although they do not solubilize biological membranes, they can, after conventional solubilization, substitute for detergents to keep membrane proteins soluble, which generally improves their stability [Breyton, Chabaud, Chaudier, Pucci and Popot (2004) FEBS Lett. 564, 312–318]. In the present study, we show that (hemi)fluorinated surfactants can be used for in vitro synthesis of membrane proteins: they do not interfere with protein synthesis, and they provide a suitable environment for MscL, a pentameric mechanosensitive channel, to fold and oligomerize to its native functional state. Following synthesis, both types of surfactants can be used to deliver MscL directly to pre-formed lipid vesicles. The electrophysiological activity of MscL synthesized in vitro in the presence of either hemi- or per-fluorinated surfactant is similar to that of the protein expressed in vivo.

scholarly journals Identification of detergent-resistant plasma membrane microdomains in dictyostelium: enrichment of signal transduction proteins.

1997 ◽  
Vol 8 (5) ◽  
pp. 855-869 ◽  
Author(s):  
Z Xiao ◽  
P N Devreotes
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Cell Surface ◽  
G Protein ◽  
Biochemical Characterization ◽  
Surface Membrane ◽  
Actin Binding ◽  
Membrane Microdomains ◽  
Immunogold Electron Microscopy ◽  
Membrane Structures

Unlike most other cellular proteins, the chemoattractant receptor, cAR1, of Dictyostelium is resistant to extraction by the zwitterionic detergent, CHAPS. We exploited this property to isolate a subcellular fraction highly enriched in cAR1 by flotation of CHAPS lysates of cells in sucrose density gradients. Immunogold electron microscopy studies revealed a homogeneous preparation of membrane bilayer sheets. This preparation, designated CHAPS-insoluble floating fraction (CHIEF), also contained a defined set of 20 other proteins and a single uncharged lipid. Cell surface biotinylation and preembedding immunoelectron microscopy both confirmed the plasma membrane origin of this preparation. The cell surface phosphodiesterase (PDE) and a downstream effector of cAR1, adenylate cyclase (ACA), were specifically localized in these structures, whereas the cell adhesion molecule gp80, most of the major cell surface membrane proteins, cytoskeletal components, the actin-binding integral membrane protein ponticulin, and G-protein alpha- and beta-subunits were absent. Overall, CHIFF represents about 3-5% of cell externally exposed membrane proteins. All of these results indicate that CHIFF is derived from specialized microdomains of the plasma membrane. The method of isolation is analogous to that of caveolae. However, we were unable to detect distinct caveolae-like structures on the cell surface associated with cAR1, which showed a diffuse staining profile. The discovery of CHIFF facilitates the purification of cAR1 and related signaling proteins and the biochemical characterization of receptor-mediated processes such as G-protein activation and desensitization. It also has important implications for the "fluid mosaic" model of the plasma membrane structures.

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