Simultaneous Identification of Unmodified Tryptic Peptides, Phosphopeptides, Glycopeptides, and Deamidated Peptides by Electrostatic Repulsion-Hydrophilic Interaction Chromatography (ERLIC)-MS/MS

摘要

Protein functions are modulated by a wide range of post-translational modifications (PTMs). Characterizing them is time-consuming if possible at all because most methods can only characterize one particular PTM per experimental run. The ERLIC mode of chromatography has recently been introduced, a combination of hydrophilic interaction and electrostatic repulsion. This mixed-mode method is especially powerful for fractionation of complex peptide digests because multiple chromatographic properties can be exploited to enhance selectivity. We present here the fractionation of unmodified peptides and the selective isolation and identification of glycosylated, phosphorylated, and deamidated peptides.