The solubilization of proteins in protein extraction and analysis requires the use of surfactants such as SDS and LDS, and denaturing agents urea and guanidine. However, the protein refolding and purification may be difficult in some cases since the interaction between surfactants and agents and proteins is strong.
The amphiphilic small compounds containing cation and anion in a molecule such as 3-[(2-hydroxyethyl)dimethylammonio]propane-1-sulfonate (NDSB 211), 3-(1-pyridinio)propanesulfonate (NDSB 201), and 3-(4-tert-butyl-1-pyridinio)propanesulfonate (NDSB 256-4T) are called non-detergent sulfobetaines (NDSB), which have different properties from general surfactants. NDSB does not form micelles because of its smaller hydrophobic moiety and can solubilize proteins mildly. Also it has been reported that NDSB has the effect of prevention of protein denaturation by heat or acid, inhibition of protein aggregation, acceleration of protein refolding, and promotion of membrane protein extract.
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Non-detergent Sulfobetaines (NDSB) Suitable for Protein Handling
Related Products
- H1399
- 3-[(2-Hydroxyethyl)dimethylammonio]propane-1-sulfonate (NDSB 211)
- S0813
- 3-(1-Pyridinio)propanesulfonate (NDSB 201)
- B4030
- 3-(4-tert-Butyl-1-pyridinio)propanesulfonate (NDSB 256-4T)
References
- A new additive for protein crystllization
- Non-detergent sulphobetaines: a new class of mild solubilization agents for protein purification
- Non-detergent sulphobetaines: a new class of molecules that facilitate in vitro protein renaturation
- Interactions of non-detergent sulfobetaines with early folding intermediates facilitate in vitro protein renaturation
- Physical–chemical features of non-detergent sulfobetaines active as protein-folding helpers
- A nondetergent sulfobetaine improves protein unfolding reversibility in microcalorimetric studies
- Inhibitory effects of choline-O-sulfate on amyloid formation of human islet amyloid polypeptide