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. This functional unit enables 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 some popular detergents.