The importance of detergents as tools for the study of membrane proteins cannot be underestimated. They are usually vital in the isolation, purification and crystallization of membrane proteins. Therefore, with the in-depth research and development of membrane proteins, detergents have also been rapidly developed. In order to find a perfect detergent to solve the many challenges such as membrane protein stability and solubility, several strategies have been used to develop novel detergents. For example, developing facial amphiphiles with a rigid core structure or to include branching points in detergent portions. Today, several novel molecules with quite unique structures and features have been developed [1]. These detergents are introduced below.
- Neopentyl-based glycosides: The detergents based on a neopentyl moiety as a central branching point for two hydrophobic alkyl chains of the same length and two glycoside groups as hydrophilic portion of the detergent. This type of detergents includes maltose neopentyl glycol amphiphiles (MNG), glucose neopentyl glycol amphiphiles (GNG), tandem neopentyl glycol maltosides (TNMs), xylene-linked maltoside amphiphiles (XMAs) and norbornane-based maltosides (NBMs) [1]. These detergents are mild and non-denaturing, because they disrupt protein-lipid and lipid-lipid interactions rather than protein-protein interactions. The hydrophilic head groups of these detergents offer ample strength to extract proteins while still providing the capability to stabilize proteins in solution and promote crystal growth. Thus, these detergents are successfully used for membrane protein crystallization. In addition, these detergents also have the ability to stabilize other large macromolecules.
Fig. 1. The structures of MNG-3 and GNG-3.
- Fluorinated detergents: Fluorinated detergents refer to the hydrogen atoms in alkyl chains of detergents structure are replaced by fluorine, which leads to enhanced chemical stability accompanied by strongly reduced polarizability and a significant volume increase and spatial extension of the rigidified fluoroalkyl backbone. It can be very useful in purification steps of membrane proteins as they do not strip natural lipids and other co-factors from the proteins.
- Tripod detergents: The tripod detergents were introduced by Yu et al. [2] and feature bulky hydrophobic groups with a tertiary carbon center carrying up to three different aliphatic or aromatic substituents. The tripod hydrophobic groups range in between of classical flexible alkyl chains and the very rigid cholic acid derivatives and could therefore provide the appropriate mixture of flexibility and stiffness required for detergents in membrane protein crystallography.
Fig. 2. The structures of tripod detergents.
- Seleniated detergents: Seleniated detergents refer to the introduction of selenium atom into existing detergent structures. A selenium atom is very dense and in X-ray diffraction studies these dense atoms are used as points of reference to overcome crystal phasing problems. Therefore, replacing current detergent that produced poor X-ray diffraction results with seleniated detergents will create reference points and help to characterize membrane proteins structure.
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Alfa Chemistry utilizes many years of academic know-how to develop high purity and high-quality novel detergents for clients all over the world. Today, we have independently developed and produced a variety of novel detergents for any application researches, including as neopentyl-based glycosides, fluorinated detergents, tripod detergents and seleniated detergents. Please click on the links below to visit our products.
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References
- Breibeck, J. and Rompel, A. Successful amphiphiles as the key to crystallization of membrane proteins: Bridging theory and practice. Biochimica Et Biophysica Acta (BBA)-General Subjects, 2019, 1863(2): 437-455.
- Yu, S. M., et al. An improved tripod amphiphile for membrane protein solubilization. Protein Science, 2000, 9(12): 2518-2527.
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