Hydrophilic interaction chromatography HILIC , peptides

Figure 3.8 Structural analysis of a post-translationally modified peptide by MALDI-MS/MS. Porcine membrane dipeptidase, a GPi-anchored glycoprotein, was in-gel-digested by trypsin. The C-terminal CPi-anchored peptide was recovered from the peptide mixture by hydrophilic interaction chromatography (HiLiC) and then analyzed...

Hydrophilic substances are soluble in water or attract water to their surfaces. Polar organic molecules have hydrophilic regions. Hydrophilic interaction chromatography (HILIC) is used to separate molecules that are too polar to be retained by reversed-phase columns. In biochemistry, HILIC is useful for separating peptides and saccharides (sugars). 

The following sections will cover various separation modes used for the characterization of proteins by UHPLC reversed-phase chromatography (RP-UHPLC) of proteins and peptide maps, RP-UHPLC for LC/MS and LC/MS/MS applications, hydrophilic interaction chromatography (HILIC) for glycan profiling, hydrophobic... 

Hydrophilic interaction liquid chromatography (HILIC) was proposed for the separation of diketopiperazines such as cyclo(Ala-Ser), cyclo(Gly-Leu), and cyclo(Ala-Gly), for carbohydrates, and nucleotides by Alpert [13]. Yoshida [14] analyzed peptides on a carbamide derivatized stationary phase. Later Strege [15] used HILIC-ESI-MS for the discovery of polar natural drugs such as vancomycin, terreic add, and cephalosporin C. 

Figure 3 Hydrophilic interaction liquid chromatography (HILIC) of a test mixture composed of amino acids and hydrophilic peptides.

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