Description
n-Dodecyl-B-D-Maltoside, or DDM, is a maltoside based non-ionic detergent with a hydrophilic maltose head and a hydrophobic long chain alkyl tail. It is considered a gentle detergent that is more efficient than other detergents, such as CHAPS or NP-40. It has a comparatively low critical micelle concentration (CMC) of 0.17mM compared to the other maltoside based detergents.
The primary attribute of DDM is its capability to extract hydrophobic proteins while maintaining the solution-phase protein conformation. DDM also allows the protein to be reformed following denaturation. Most membrane-bound proteins are α-helix bundles, which are less robust to changes in their cellular environment. DDM offers a detergent capable of preserving these proteins. This is in contrast to other, harsher ionic detergents that destabilize and permanently denature α-helical membrane-bound proteins. DDM has been used to solubilize the multidrug-transporter protein, EmrE, as well as the nucleoside-specific porin protein, Tsx.
DDM has also been shown in several cases to facilitate a high degree of reactivation of previously denatured enzymes, possibly due to weak bonding between DDM and intermediate conformational isomers.
Common Applications:
(Click each for more information)
Solubilization of Membrane Proteins for Structural Biology
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Purpose: To extract and stabilize membrane proteins in a functional form for crystallography or cryo-EM studies.
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How It Works: DDM is a mild nonionic detergent that disrupts lipid bilayers while preserving protein conformation and activity. Its long alkyl chain and maltoside headgroup provide a stable micelle environment ideal for protein solubilization.
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Applications: Used to isolate GPCRs, ion channels, and transporters for X-ray crystallography or cryo-electron microscopy.
Carpenter, E. P., Beis, K., Cameron, A. D., & Iwata, S. (2008). Overcoming the challenges of membrane protein crystallography. Curr Opin Struct Biol, 18(5), 581–586. doi:10.1016/j.sbi.2008.07.001
Reconstitution of Membrane Proteins into Lipid Bilayers or Nanodiscs
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Purpose: To incorporate purified membrane proteins into artificial lipid systems for functional studies.
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How It Works: DDM-solubilized proteins are transferred into liposomes or nanodiscs by removing detergent via dialysis or absorbents, recreating a native-like lipid environment.
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Applications: Used in transport assays, electrophysiology, or ligand-binding studies.
Denisov, I. G., Grinkova, Y. V., Lazarides, A. A., & Sligar, S. G. (2004). Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size. PNAS, 101(11), 3890–3895. doi:10.1073/pnas.0400046101
Detergent Screening in Membrane Protein Optimization
Key Benefits:
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Gentle and effective membrane solubilization: Preserves native protein function and structure.
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Forms stable protein–detergent micelles: Minimizes aggregation and supports purification and structural studies.
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Low absorbance background: Reduces interference in UV-based protein quantification and optical assays.
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Established standard in structural biology: Extensively used for crystallography and cryo-EM sample preparation of membrane proteins.
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Compatible with reconstitution and assay systems: Enables functional analysis in native-like environments.
Product Specifications
Molecular Formula: C24H46O11
Molecular Weight: 510.63 g/mol
PubChem Chemical ID: 114880
Storage/Handling:
Store at -15oC. Protect from light
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