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Creative Biolabs provides high-quality membrane protein production services using Mempro™ detergent-free production. We are capable of satisfying your specific demands in membrane protein production.
Detergent can disrupt the phospholipids into small micelles and induce membrane protein inactivation during conventional membrane protein production using water-soluble (detergent-lipid-protein) complex. Creative Biolabs offers an alternative strategy, after the solubilization process of membrane protein production, to keep membrane protein soluble in water in the absence of detergent. Furthmore, detergent-free production of membrane protein with native-like membrane environment and active protein has signifant advantage in structural and functional determinations. We can employ several approaches to perform Mempro™ detergent-free membrane protein production.
Nanodiscs are the self-assembly and disc-like nanotechnological systems, which can stabilize membran proteins removed from the membrane by membrane scaffold proteins (MSPs) in no need of detergent (Figure 1). This technology is widely used for solubilization and characterization of integral membrane proteins.
Figure 1. Model of a nanodisc with an reconstituted transmembrane protein. (J. Nanobiotechnology, 2010)
Amphipols (especially A8-35) can replace the detergent used to keep membrane proteins in aqueous solutions. The amphipathic amphipols have the ability to “trap” around transmembrane regions of proteins, allowing them to stay folded (Figure 2). The amphipols can be applied in electron microscopy (EM), nuclear magnetic resonance (NMR), in vitro functional analysis and other potential utilizations.
Figure 2. Comparison between amphipols and detergents. (Trends Biotechnol., 2011)
Poly(styrene-co-maleic acid) lipid particles (SMALPs) can reversibly encapsulate the membrane proteins (Figure 3). The polymer itself is made of alternating hydrophilic (maleic acid) and hydrophobic (styrene) moieties. The SMALPs are self-assembled by the simple addition of the SMA co-polymer. SMALPs are ideally suited to purification and further biochemical studies (such as drug discovery) due to its characterisctics of high temperature resistance and pH sensitivity.
Figure 3. Diagrammatic representation of a disc-like SMALP (Physwiki).
These novel detergent-free methodologies mean that membrane proteins can be obtained easily, and enabling more comprehensively structural and functional studies on membrane proteins.
C. Tribet, et al. (1996). Amphipols: Polymers that keep membrane proteins soluble in aqueous solutions. Proc Natl Acad Sci U. S. A. 93: 15047-15050.
J.L. Baneres, et al. (2011). New advances in production and functional folding of G-protein-coupled receptors. Trends Biotechnol. 29(7): 314-322.
M. Jamshad, et al. (2011). Surfactant-free purification of membrane proteins with intact native membrane environment. Biochem. Soc. Trans. 39: 813-818.
R.O. Ryan, (2010). Nanobiotechnology applications of reconstituted high density lipoprotein. J. Nanobiotechnol 8(1):28-37.
SMALP Technology. (http://physwiki.ucdavis.edu/Wikitexts/UCD_BPH241/SMALP_Technology).
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