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Detergent Purification of Membrane Proteins

Detergent Purification of Membrane Proteins

Detergents are used to purify the integral proteins of the membrane. The hydrophobic portion of the detergent can replace membrane phospholipids while solubilizing the membrane proteins. When detergent monomers reach a specific concentration in a solution called critical micelle concentration (CMC), they form micelles. Above CMC, the concentration of the detergent monomers remains in equilibrium with the micelle. The number of detergent monomers present in the CMC varies for each detergent, and...

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Updated: Apr 16, 2026

Green Fluorescent Protein-based Expression Screening of Membrane Proteins in Escherichia coli

Green Fluorescent Protein-based Expression Screening of Membrane Proteins in Escherichia coli

Published on: January 6, 2015

A fluorinated detergent for membrane-protein applications.

Erik Frotscher¹, Bartholomäus Danielczak, Carolyn Vargas

¹Molecular Biophysics, University of Kaiserslautern, Erwin-Schrödinger-Str. 13, 67663 Kaiserslautern (Germany).

Angewandte Chemie (International Ed. in English)

|March 11, 2015

Summary

Fluorinated surfactants can be detergents. A novel compound, F6 OM, solubilizes membranes gently and aids integral membrane enzyme refolding, unlike other fluorinated surfactants.

Keywords:

biomembranes liposomes micelles proteins surfactants

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Detergent-free Ultrafast Reconstitution of Membrane Proteins into Lipid Bilayers Using Fusogenic Complementary-charged Proteoliposomes.

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Published on: April 5, 2018

Area of Science:

Biochemistry
Membrane Biophysics
Surfactant Chemistry

Background:

Fluorocarbon-chain surfactants offer gentle alternatives to hydrocarbon detergents for membrane protein handling.
The inertness of fluorinated surfactants limits their detergent-like activity and application in specific scenarios.

Purpose of the Study:

To investigate if fluorination precludes detergency in surfactants.
To evaluate a novel fluorinated octyl maltoside derivative (F6 OM) for its membrane interaction and solubilization properties.
To assess the efficacy of F6 OM in chaperoning integral membrane enzyme refolding.

Main Methods:

Characterization of F6 OM's interaction with phospholipid vesicles.
Assessment of membrane solubilization and order.
Comparative analysis of F6 OM and a lipophobic fluorinated surfactant in enzyme refolding.

Main Results:

F6 OM, a nonionic fluorinated surfactant, effectively solubilizes phospholipid vesicles.
F6 OM exhibits detergency without compromising membrane order at subsolubilizing concentrations.
F6 OM outperforms a lipophobic fluorinated surfactant in promoting bilayer insertion for enzyme refolding.

Conclusions:

Fluorination does not inherently prevent detergency in surfactants.
F6 OM demonstrates a mild and unique mode of detergency, enabling membrane protein handling and functional refolding.
F6 OM shows promise for applications requiring gentle yet effective membrane solubilization and protein refolding.