Significantly Improved In-Solution Tryptic Digestion of Proteins
Enzymatic digestion of proteins is an integral part of mass spectrometric characterization of proteins. Hydrophobic proteins are difficult to identify by mass spectrometric methods in part due to their low solubility and inefficient enzymatic digestion. Ionic surfactants such as SDS disrupts the aggregations of proteins, but inhibits the trypsin activity and interferes with mass spectrometric analysis. We employed a surfactant-like reagent to aid tryptic digestion of proteins. This reagent is easily removed under acidic conditions prior to MS analysis. Our preliminary results suggest that this reagent does not inhibit trypsin activities, hence drastically improves protein digestions in terms of speed and peptide recovery.