Calixarene Surfactants
G-Biosciences offers specially formulated reagents (detergents/surfactants) to aid the extraction, stabilization and crystallization of therapeutic integral membrane protein targets or antigens (while preserving their native three dimensional structure and function).
- No refolding
- No mutagenesis/truncation/fusion
- Striking stability improvement
- High purity
- Maintain functional and structural integrities
Traditional detergents do not stabilize membrane domains as efficiently as natural lipids in membranes, which often leads to a partial to complete loss of activity/stability during protein extraction and purification and preventing crystallization in an active conformation.
In contrast, G-Biosciences’ offers two varieties of innovative and customized surfactants that adapt to the biochemical characteristics of the target during the solubilization/purification/stabilization steps:
- Calixarene surfactants
- These molecules are designed to structure the membrane domains of proteins through hydrophobic interactions and a network of salt bridges with the basic residues found at the cytosol-membrane interface of membrane proteins.
- Fluorinated poly(tris) and bis-glucose surfactants
- Fluorinated surfactants are unable to extract proteins from membrane, but are useful for membrane protein stabilization in subsequent purification steps as they do not strip natural lipids and other co-factors from the proteins. In addition, the bulky fluorinated tails can not penetrate into the interior and disrupt structure. Fluorinated surfactants often decrease non-specific aggregation and are thought to result in improved distribution on cryo-EM grids and better vitrification for cryo-EM data collection. They are also reported to increase crystallizability.
- The bis-glucose compounds have a tetradhedral chiral carbon with two polar headgroups (the glucose moieties) and a long hydrophobic fluorinated tail. In this way they resemble the neo-pentyl glycol detergents, such as LMNG that have seen some recent success in structural biology.
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