An Overview of the Top Ten Detergents Used for Membrane Protein Crystallization

Artem Stetsenko,Albert Guskov

doi:10.3390/cryst7070197

Abstract

To study integral membrane proteins, one has to extract them from the membrane—the step that is typically achieved by the application of detergents. In this mini-review, we summarize the top 10 detergents used for the structural analysis of membrane proteins based on the published results. The aim of this study is to provide the reader with an overview of the main properties of available detergents (critical micelle concentration (CMC) value, micelle size, etc.) and provide an idea of what detergents to may merit further study. Furthermore, we briefly discuss alternative solubilization and stabilization agents, such as polymers.

Highlights

Every cell is encircled by the semipermeable membrane, to protect the cell content from the environment, and to differentiate it externally from the other cells, and internally to form the dedicated organelles within the cell
December 2016) and manually extracted information regarding what kind of detergent was used for purification and crystallization
Looking at the results of the performed analysis, one can confidently say that the sugar-based detergents rule the field of structural studies on membrane proteins

Summary

Introduction

Every cell is encircled by the semipermeable membrane (often termed as the lipid bilayer), to protect the cell content from the environment, and to differentiate it externally from the other cells, and internally to form the dedicated organelles within the cell This forced evolution to design a myriad of membrane-embedded and associated proteins, which are essential for the transport of charged and large chemicals in and out of the cell (since they either cannot pass or diffuse too slowly across the membrane) and for communication between adjacent cells. The most widely used agents for membrane protein extraction and stabilization are detergents, the amphiphatic molecules, bearing a hydrophilic headgroup (typically polar, sometimes charged) and a hydrophobic (apolar) tail Due to this nature, detergents are capable of inserting their hydrophobic tails into the lipidic membrane, disrupting the latter and eventually (with an increasing concentration of detergent) extracting membrane-embedded proteins (Figure 1)

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Results

Conclusion