Project: Retention mechanism of glycopeptides in hydrophilic interaction liquid chromatography
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Because protein glycosylation is one of the most frequent post-translational modifications involved in several biological processes, reliable analytical methods are necessary to understand their biofunctions. A standard technique of glycoproteomics analysis is liquid chromatography coupled to mass spectrometry (LC-MS). Although mass spectrometry is a strong tool in glycoproteins analysis, positive ionization mode of MS usually does not allow comprehensive characterization of glycopeptide structures due to similar fragmentation patterns using collision-induced dissociation. Therefore, it is essential to connect MS with chromatographic separation to achieve efficiently resolution of the analytes and to allow their quantification in complex samples. A suitable chromatographic mode for separation of glycopeptides is hydrophilic interaction liquid chromatography (HILIC). The aim of this project is to conduct an up-to-now missing systematic study of HILIC retention mechanisms of glycopeptides. Understanding and explaining HILIC mechanisms in glycoproteomics may enable us to select suitable chromatographic conditions for the separation of glycopeptides and of their isomers. In addition, the knowledge of retention mechanisms of glycopeptides in HILIC can be used to predict their relative retention time windows. This information can be helpful for reliable assignments of site-specific glycoforms of proteins and can be incorporated into glycoproteomics search engines as an additional qualitative parameter for improved glycopeptide identification.
Deadline is closed