Product Spotlight: Exclusive Detergents

Posted on February 16, 2021

Protein Crystallography

Avanti is in no short supply of products to aid in your projects and applications. This month, we are taking a closer look at Avanti’s Exclusive Detergents for your protein crystallography research.

What makes this set of detergents exclusive?

Avanti currently offers several detergents that have been exclusively licensed for manufacturing and commercial distribution. Since Avanti has an exclusive license for these chemical detergents, you won’t be able to find them anywhere else. As always these detergents are synthesized to the Avanti purity standard that you rely on when conducting your research.

Why use these exclusive detergents?

The use of detergents to encapsulate the surface of membrane proteins has been studied for several years. The large number of detergents used in membrane protein research has led to the crystallization and characterization of thousands of membrane proteins. Even with the large numbers of detergents that have been developed and utilized, there are thousands of membrane proteins that have yet to be crystallized and characterized. This is not due to a lack of effort, but rather that the vast majority of detergents are insufficient at maintaining the integrity of membrane proteins to allow crystallization. The exclusive detergents that Avanti offers have been developed to solve this issue and allow for better and more reliable membrane protein crystallization.

What makes these detergents different?

One major problem with extracting membrane proteins into a non-native environment is that it leads to rapid denaturation and aggregation of the protein. This is due to the difference and incompatibility of the hydrophobic surface of the protein and the polarity of the aqueous media used to extract the protein. Detergents have been used extensively to solve this problem. The most common detergents used for membrane protein extraction are octyl glucopyranoside (OG), nonyl glucopyranoside (NG), decyl maltoside (DM), dodecyl maltoside (DDM), and lauryldimethylamine-N-oxide (LDAO). These detergents have been fairly successful and have yielded ~70% of known "helical membrane protein structures". But even these detergents are prone to structural degradation of the membrane proteins upon extraction into aqueous media.

Detergents have typically been simple in architecture with limited variability. Membrane proteins are widely variable with regards to their 3D structures. In the last several years, research has been focused on producing novel amphiphiles with unique structures in an attempt to solubilize and stabilize membrane proteins that have previously been difficult to extract and crystallize. Avanti’s exclusive detergents take advantage of some of the most promising features in recent structural developments of detergents such as facial amphiphile detergents (FAÇADE) and neopentyl glycol (NPG) derived detergents. Many of these exclusive detergents have one or more quaternary carbon atoms enabling the incorporation of two hydrophilic and two lipophilic subunits per quaternary carbon unit. This leads to subtle restraints on conformational flexibility and properties differing from those displayed by conventional detergents.

These detergents have been evaluated and shown to have improved characteristics when compared to popular detergents such as DDM. Characteristics that have been proven to be improved in Avanti’s exclusive detergents include the critical micelle concentration (CMC), hydrodynamic radii, and hydrophile-lipophile balance (HLB). These improved characteristics show the potential for these detergents to offer enhanced protein stabilizing efficacy compared to other popular detergents.

Check out Avanti’s selection of Exclusive Detergents for crystal clear protein research!

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If you’re looking for the highest quality lipids for your next research project, look no further than Avanti’s product catalog. Browse our extensive collection of research, and feel free to reach out to us if you have any questions!