Facade®-TFA1 Detergent

Facade^®-TFA1

A crucial part of cellular physiology is the existence of membrane proteins. They"re part of many cellular processes and are more difficult to study than soluble proteins due to their relative instability. At times, they can lose structural and functional integrity after being extracted from native membranes. This presents unique challenges on the part of researchers.

Typically, conventional detergents, including n-dodecyl-β-D-maltoside (DDM), n-octyl-β-D-glucoside (OG), and lauryldimethylamine-N-oxide (LDAO) are used in the extraction, purification, and crystallization of membrane proteins due to their ability to protect the large hydrophobic protein surfaces from the polar aqueous environment. The problem with this is that these detergents tend to suffer from protein denaturation and aggregation over time. The majority of them are limited in their structural variation because of their common characteristics of having a polar head group and a long flexible tail group.

Novel Agents for Membrane Protein Study

Multiple classes of novel agents have entered the ring over the past twenty years. Polymeric materials such as amphipols and styrene-maleic acid copolymer (SMA), and nanoassemblies (e.g., nanodiscs (NDs)) have been successfully applied to membrane protein study.

Small amphipathic compounds are another major group of novel agents, a class that includes tripod amphiphiles (TPAs), neopentyl glycol (NG) class amphiphiles (MNGs/GNGs/NDT), glyco-diosgenin (GDN), fluorinated detergents (F6OM), penta-saccharide amphiphiles (PSEs), mannitol-based amphiphiles (MNAs), dendronic trimaltosides (DTMs), and glycosyl-substituted dicarboxylate detergents (DCODs). Some of these agents, including MNG-3 and GNG-3, are widely used in membrane protein structural study.

Conventional detergents, like DDM, have been the “gold standard” for target membrane proteins in research. However, new research has unearthed other potential candidates that rival, if not surpass, ineffectiveness.

For instance, TFA-1 previously produced two non-facial rotamers as evidenced by HNMR spectrum at room temperature. The presence of these two non-facial rotamers posed a significant problem: This presence restricts the facial property of TFA-1 in solution and (likely) its ability to stabilize membrane proteins.

Owing to this, Avanti’s research altered TFA-1 in three key ways: we increased water solubility through new amphiphilic creation via cholate-tris-maltoside, we connected building blocks via non-polar ether-based linkers, and we introduced a few different linkers to produce new facial amphiphiles with a diverse set of hydrophobic lengths. This aforementioned TFA-1 provides an excellent control condition to test for the effect of amide and ether linkages on protein stability, which allowed for even more membrane protein stability experimentation. In the study, TFA-1 overtook TFM-C3Am in transporter stabilization.

The ongoing study suggests the significance of detergent hydrophobic length in protein stability. Facade®-TFA1/tandem facial amphiphiles (TFAs) provide the required length for membrane stabilization. Due to their ability to be produced in mass quantities, they are highly viable candidates for membrane protein research.

Using Facade®-TFA1 from Avanti Polar Lipids

Avanti Polar Lipids offers only the best quality lipids for your research. Our Facade®-TFA1 facial amphiphiles (TFAs) comprise a pair of maltose-functionalized deoxycholate units and are used in the stabilization of membrane proteins.

Purchase high-quality, high-purity Facade®-TFA1 here!

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• 3D Structure
• Structure
• Safety Data Sheet