The benefits of hybrid fragmentation methods for glycoproteomics

Publication date: Available online 17 September 2018Source: TrAC Trends in Analytical ChemistryAuthor(s): Karli R. Reiding, Albert Bondt, Vojtech Franc, Albert J.R. HeckAbstractGlycosylation is an important and variable protein modification that can have a profound effect on the physiological characteristics of the substrate, warranting careful examination in applications ranging from the development and quality control of biopharmaceuticals to clinical glycoproteomics.Glycoproteomics describes the mass spectrometric analysis of protein glycosylation in a site-specific manner, typically of proteolytically digested glycoprotein samples. This may be achieved by interpreting the mass (over charge) values of (glyco)peptides across a run of liquid chromatography coupled to mass spectrometry (LC-MS), and acquiring the fragmentation patterns of selected precursors to sequence the peptide and characterize the composition/structure of the glycan. It has become apparent, however, that most fragmentation mechanisms do not equivalently affect the glycan and peptide portion of a glycopeptide. For example, collision-induced dissociation (CID) and higher-energy collisional dissociation (HCD) primarily yield abundant B- and Y-ions from the glycan portion of a glycopeptide conjugate, whereas electron-transfer dissociation methods such as electron-capture dissociation (ECD) and electron-transfer dissociation (ETD) mainly affect the peptide backbone to yield c- and z-ions.Hybrid fragmentation, ...
Source: TrAC Trends in Analytical Chemistry - Category: Chemistry Source Type: research
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