A novel SDS analog compatible with MS analysis of proteins and peptides

Library Number:
Part Number:
Compton, Bruce J.;Lee, Jeng-Jong;Brown, Elizabeth K.;Herbert, Robert G.;Ding, Jianmei;Livingstone, Jeff;Bouvier, Edouard S.
1999 ASMS
Content Type:
Content Subtype:
Proteins, Peptides
Protein solubilization and purification often necessitates the use of surfactants. However, surfactants cause ion suppression in mass spectrometric detection. In particular, ionic detergents such as sodium dodecyl sulfate (SDS) which are routinely used as denaturing reagents for proteins in SDS-polyacrylamide gel electrophoresis (PAGE), must be removed from the sample prior to the MS analysis. While a variety of techniques such as electroblotting, electroelution, on-line dialysis and on-line adsorption have been developed to remove deleterious interferences, execution of these steps on minute sample quantities inevitable results in sample loss. The most common approach to removing SDS is to electroblot a protein onto a membrane using a suitable solvent. This technique is time-consuming and can result in significant protein loss due to strong non-specific interactions with the membrane, particularly for hydrophobic proteins and peptides. In order to eliminate these problems, we have developed acid-labile anionic surfactants (ALS) that can be used as replacements for SDS in protein solubilization and Laemmli gels. These surfactants are compatible with electrospray with matrix assisted laser desorption ionization methods, and no electroblotting or electroelution is needed prior to the MS analysis. MS data of proteins which are purified by PAGE using both SDS and the novel acid-labile surfactants are compared, demonstrating an enhancement in detection when using the latter surfactants.

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