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

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 DNA-Machinery for Delivering Membrane Proteins into Free Standing Lipid Bilayers

2011 ◽  
Vol 100 (3) ◽  
pp. 633a
Author(s):  
Minsub Chung ◽  
Poul Martin Bendix ◽  
Namdoo Kim ◽  
Steven G. Boxer
Keyword(s):  
Membrane Proteins ◽  
Lipid Bilayers ◽  
Free Standing

scholarly journals Synthesis and application of non-bioaccumulable fluorinated surfactants: a review

2021 ◽  
Vol 3 (1) ◽  
Author(s):  
Rong Zhou ◽  
Yong Jin ◽  
Yichao Shen ◽  
Peng Zhao ◽  
Yutang Zhou
Keyword(s):  
Sustainable Development ◽  
Membrane Proteins ◽  
Emulsion Polymerization ◽  
Perfluorooctane Sulfonate ◽  
Industrial Applications ◽  
Negative Effects ◽  
Fluorinated Surfactants ◽  
Structure Activity ◽  
Weak Points ◽  
Fluorocarbon Chain

Abstract Due to negative effects of conventional fluorinated surfactants with long perfluorocarbon chain (CxF2x+ 1, x≥7) like perfluorooctanoic acid (PFOA) and perfluorooctane sulfonate (PFOS), these conventional long perfluorocarbon chain surfactants have been restricted in many industrial applications. Nowadays, their potential non-bioaccumulable alternatives have been developed to meet the requirements of environmental sustainable development. In this paper, the recent advances of potential non-bioaccumulable fluorinated surfactants with different fluorocarbon chain structures, including the short perfluorocarbon chain, the branched fluorocarbon chain, and the fluorocarbon chain with weak points, are reviewed from the aspects of synthesis processes, properties, and structure-activity relationships. And their applications in emulsion polymerization of fluorinated olefins, handling membrane proteins, and leather manufacture also are summarized. Furthermore, the challenges embedded in the current non-bioaccumulable fluorinated surfactants are also highlighted and discussed with the hope to provide a valuable reference for the prosperous development of fluorinated surfactants. Graphical abstract

Stabilization of integral membrane proteins in aqueous solution using fluorinated surfactants

Biochimie ◽  
1998 ◽  
Vol 80 (5-6) ◽  
pp. 515-530 ◽  
Author(s):  
E. Chabaud ◽  
P. Barthélémy ◽  
N. Mora ◽  
J.L. Popot ◽  
B. Pucci
Keyword(s):  
Aqueous Solution ◽  
Membrane Proteins ◽  
Integral Membrane Proteins ◽  
Fluorinated Surfactants

scholarly journals Fluorinated Surfactants for Structural Studies of Membrane Proteins

2012 ◽  
Vol 102 (3) ◽  
pp. 289a
Author(s):  
Christine Ebel ◽  
Cécile Breyton ◽  
Frank Gabel ◽  
Maher Abla ◽  
Florence Lebaupain ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Structural Studies ◽  
Fluorinated Surfactants

scholarly journals Interactions of Fluorinated Surfactants with Diphtheria Toxin T-Domain: Testing New Media for Studies of Membrane Proteins

2008 ◽  
Vol 94 (11) ◽  
pp. 4348-4357 ◽  
Author(s):  
Mykola V. Rodnin ◽  
Yevgen O. Posokhov ◽  
Christiane Contino-Pépin ◽  
Joshua Brettmann ◽  
Alexander Kyrychenko ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
New Media ◽  
Diphtheria Toxin ◽  
Fluorinated Surfactants ◽  
T Domain

Changes Occur in Plasma Membrane Turnover when K562 Leukemia Cells are Induced to Differentiate

1982 ◽  
Vol 40 ◽  
pp. 286-287
Author(s):  
L. M. Marshall
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Intracellular Transport ◽  
Parent Cell ◽  
Membrane Turnover ◽  
Coated Pits ◽  
Surface Distribution ◽  
Specific Proteins ◽  
Erythroleukemic Cell ◽  
Specific Membrane

A human erythroleukemic cell line, metabolically blocked in a late stage of erythropoiesis, becomes capable of differentiation along the normal pathway when grown in the presence of hemin. This process is characterized by hemoglobin synthesis followed by rearrangement of the plasma membrane proteins and culminates in asymmetrical cytokinesis in the absence of nuclear division. A reticulocyte-like cell buds from the nucleus-containing parent cell after erythrocyte specific membrane proteins have been sequestered into its membrane. In this process the parent cell faces two obstacles. First, to organize its erythrocyte specific proteins at one pole of the cell for inclusion in the reticulocyte; second, to reduce or abolish membrane protein turnover since hemoglobin is virtually the only protein being synthesized at this stage. A means of achieving redistribution and cessation of turnover could involve movement of membrane proteins by a directional lipid flow. Generation of a lipid flow towards one pole and accumulation of erythrocyte-specific membrane proteins could be achieved by clathrin coated pits which are implicated in membrane endocytosis, intracellular transport and turnover. In non-differentiating cells, membrane proteins are turned over and are random in surface distribution. If, however, the erythrocyte specific proteins in differentiating cells were excluded from endocytosing coated pits, not only would their turnover cease, but they would also tend to drift towards and collect at the site of endocytosis. This hypothesis requires that different protein species are endocytosed by the coated vesicles in non-differentiating than by differentiating cells.

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