Perfluoroalkylphosphocholines are poor protein-solubilizing surfactants, as tested with neutrophil plasma membranes

Mardirossian, C Der; Krafft, Marie Pierre; Gulik-Krzywicki, T.; Maire, Marc le; Lederer, Florence

doi:10.1016/s0300-9084(00)80018-8

Cited by 23 publications

(13 citation statements)

References 59 publications

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“…Solubilization of 0.1 mm POPC LUVs required several days at 2 mm F 6 OM and 25 8C but was greatly accelerated by increasing the surfactant concentration to 10 mm (Figure 2 b) or raising the temperature to 60 8C (Figure 2 c). [15] These differences in solubilizing power rationalize the observation that F 6 OPC but not F 6 OM is compatible with free-standing lipid bilayers. [15] These differences in solubilizing power rationalize the observation that F 6 OPC but not F 6 OM is compatible with free-standing lipid bilayers.…”

Section: Methodsmentioning

confidence: 62%

“…[7] By analogy to the poor miscibility of liquid hydrocarbons and fluorocarbons, contacts between fluorinated surfactant tails and hydrocarbon moieties of proteins and lipids are expected to be unfavorable, such that structurally or functionally important protein/protein and protein/ lipid interactions are not disrupted. [7,12] The peculiarity of fluorocarbon chains of being both hydrophobic and lipophobic is thought not only to prevent protein denaturation and delipidation but also to render fluorinated surfactants poor solubilizers [13][14][15][16][17][18] unless they contain a harsh, ionic headgroup. [7,12] The peculiarity of fluorocarbon chains of being both hydrophobic and lipophobic is thought not only to prevent protein denaturation and delipidation but also to render fluorinated surfactants poor solubilizers [13][14][15][16][17][18] unless they contain a harsh, ionic headgroup.…”

mentioning

confidence: 99%

“…[12,13] Moreover, fluorocarbon chains are bulkier than their hydrocarbon counterparts, which prevents them from intruding between protein transmembrane domains. [7,12] The peculiarity of fluorocarbon chains of being both hydrophobic and lipophobic is thought not only to prevent protein denaturation and delipidation but also to render fluorinated surfactants poor solubilizers [13][14][15][16][17][18] unless they contain a harsh, ionic headgroup. [19] Herein, we show that, contrary to this assumption, nonionic fluorinated surfactants can be powerful yet mild detergents.…”

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confidence: 99%

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A Fluorinated Detergent for Membrane‐Protein Applications

et al. 2015

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Surfactants carrying fluorocarbon chains hold great promise as gentle alternatives to conventional hydrocarbon-based detergents for the solubilization and handling of integral membrane proteins. However, their inertness towards lipid bilayer membranes has limited the usefulness of fluorinated surfactants in situations where detergent-like activity is required. We demonstrate that fluorination does not necessarily preclude detergency, as exemplified by a fluorinated octyl maltoside derivative termed F6 OM. This nonionic compound readily interacts with and completely solubilizes phospholipid vesicles in a manner reminiscent of conventional detergents without, however, compromising membrane order at subsolubilizing concentrations. Owing to this mild and unusual mode of detergency, F6 OM outperforms a lipophobic fluorinated surfactant in chaperoning the functional refolding of an integral membrane enzyme by promoting bilayer insertion in the absence of micelles.

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Section: Methodsmentioning

confidence: 62%

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confidence: 99%

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confidence: 99%

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A Fluorinated Detergent for Membrane‐Protein Applications

et al. 2015

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“…By the same token, however, fluorinated surfactants can be expected to be poorly efficient at preventing membrane proteins from aggregating. The latter prediction was fulfilled in experiments that we [19,20] and others [21–23] carried out some years ago. In brief, these early attempts in general showed that fluorinated surfactants were unable not only to solubilize membrane proteins, but also to maintain them in solution after they had been extracted from membranes using a classical detergent.…”

Section: Introductionmentioning

confidence: 61%

Hemifluorinated surfactants: a non‐dissociating environment for handling membrane proteins in aqueous solutions?

et al. 2004

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The instability of membrane proteins in detergent solution can generally be traced to the dissociating character of detergents and often correlates with delipidation. We examine here the possibility of substituting detergents, after membrane proteins have been solubilized, with non-detergent surfactants whose hydrophobic moiety contains a per£uorinated region that makes it lipophobic. In order to improve its a⁄nity for the protein surface, the £uorinated chain is terminated by an ethyl group. Test proteins included bacteriorhodopsin, the cytochrome b 6 f complex, and the transmembrane region of the bacterial outer membrane protein OmpA. All three proteins were puri¢ed using classical detergents and transferred into solutions of C 2 -H 5 C 6 F 12 C 2 H 4 -S-poly-Tris-(hydroxymethyl)aminomethane (HF-TAC). Transfer to HF-TAC maintained the native state of the proteins and prevented their precipitation. Provided the concentration of HF-TAC was high enough, HF-TAC/membrane protein complexes ran as single bands upon centrifugation in sucrose gradients. Bacteriorhodopsin and the cytochrome b 6 f complex, both of which are detergent-sensitive, exhibited increased biochemical stability upon extended storage in the presence of a high concentration of HF-TAC as compared to detergent micelles. The stabilization of cytochrome b 6 f is at least partly due to a better retention of protein-bound lipids. ß

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“…So they were applied in temporary blood substitutes or drug delivery systems [13]. Various results of membrane proteins solubilizing properties were obtained with different types of fluorinated amphiphiles such as perfluorophosphocholines [14,15]. However, some of these surfactants get progressive interest for their ability to maintain the native state of the proteins [16,17] and prevent their precipitation [18].…”

Section: Introductionmentioning

confidence: 99%

2‐DE using hemi‐fluorinated surfactants

et al. 2007

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The synthesis of hemi-fluorinated zwitterionic surfactants was realized and assessed for 2-DE, a powerful separation method for proteomic analysis. These new fluorinated amidosulfobetaine (FASB-p,m) were compared to their hydrocarbon counterparts amidosulfobetaine (ASB-n) characterized by a hydrophilic polar head, a hydrophobic and lipophilic tail, and an amido group as connector. The tail of these FASB surfactants was in part fluorinated resulting in the modulation of its lipophilicity (or oleophobicity). Their effect on the red blood cell (RBC) membrane showed a specific solubilization depending on the length of the hydrophobic part. A large number of polypeptide spots appeared in the 2-DE patterns by using FASB-p,m. The oleophobic character of these surfactants was confirmed by the fact that Band 3, a highly hydrophobic transmembrane protein, was not solubilized by these fluorinated structures. The corresponding pellet was very rich in Band 3 and could then be solubilized by using a strong detergent such as amidosulfobetaine with an alkyl tail containing 14 carbon atoms (ASB-14). Thus, these hemi-fluorinated surfactants appeared as powerful tools when used at the first step of a two-step solubilization strategy using a hydrocarbon homologous surfactant in the second step.

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Perfluoroalkylphosphocholines are poor protein-solubilizing surfactants, as tested with neutrophil plasma membranes

Cited by 23 publications

References 59 publications

A Fluorinated Detergent for Membrane‐Protein Applications

A Fluorinated Detergent for Membrane‐Protein Applications

Hemifluorinated surfactants: a non‐dissociating environment for handling membrane proteins in aqueous solutions?

2‐DE using hemi‐fluorinated surfactants

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