Label-free quantitation: A new glycoproteomics approach |
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Authors: | Kathryn R Rebecchi Jamie L Wenke Eden P Go Heather Desaire |
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Institution: | 1. Department of Chemistry, University of Kansas, 1251 Wescoe Hall Drive, 66045, Lawrence, KS
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Abstract: | We demonstrate herein a method for quantifying glycosylation changes on glycoproteins. This novel method uses MS data of characterized
glycopeptides to analyze glycosylation profiles, and several quality control tests were done to demonstrate that the method
is reproducible, robust, applicable to different types of glycoproteins, and tolerant of instrumental variability during ionization
of the analytes. This method is unique in that it is the first label-free quantitative method specifically designed for glycopeptide
analysis. It can be used to monitor changes in glycosylation in a glycosylation site-specific manner on a single glycoprotein,
or it can be used to quantify glycosylation in a glycoprotein mixture. During mixture analysis, the method can discriminate
between changes in glycosylation of a given protein, and changes in the glycoprotein’s concentration in the mixture. This
method is useful for quantitative analyses in biochemical studies of glycoproteins, where changes in glycosylation composition
can be linked to functional differences; it could also be implemented in the pharmaceutical industry, where glycosylation
profiles of glycoprotein-based therapeutics must be quantified. Finally, quantification of glycopeptides is an important aspect
of glycopeptide-based biomarker discovery, and our quantitative approach could be a valuable asset to this field as well,
provided the compositions of the glycopeptides to be quantified are identifiable using other methods. |
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