Work

Predicting the HILIC Retention Behavior of the N-Linked Glycopeptides Produced by Trypsin Digestion of Immunoglobulin Gs (IgGs)

Year: 2018

Type: article

Abstract: The prediction of the retention behavior/time would facilitate the identification and characterization of glycoproteins, particularly the analytical challenges, such as the characterization of low-abundance glycoforms. This task is essential in the biotherapeutics industry, where the type and amount of glycosylation on recombinant IgG alter the efficacy, function, and immunogenicity. Models exist for the prediction of the hydrophilic interaction liquid chromatography retention of peptides and glycans. Here, we have devised a unified model to predict the retention behavior of glycopeptides from human IgGs and applied this to the analysis of glycopeptides from rabbit IgGs. The combined model is capable of accurately predicting the retention of native IgG glycopeptides on 2 completely different liquid chromatography-mass spectrometry systems.

Source: Journal of Biomolecular Techniques JBT

DOI: 10.7171/jbt.18-2904-002

Authors: Majors J. Badgett, Emily Mize, Tyler Fletcher, Barry Boyes, Ron Orlando

Institutions: University of Georgia, Advanced Materials Technology (United States)

Language: English

Topic: Glycosylation and Glycoproteins Research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: diamond

Funders: National Institutes of Health, National Institute of General Medical Sciences

Awards: Development of Isotopically Labeled Glycoproteins for use as Internal Standards, Development of Isotopically Labeled Glycoproteins for use as Internal Standards, Novel Materials and Methods for Separations of Glycopeptides and Glycans, Generation of antibodies to monitor Notch O-fucosylation in vivo