N-glycosylation is a post-translational modification (PTM) that plays a crucial role in monoclonal antibody (mAb) effector functions and is, therefore, classified as a critical quality attribute (CQA) that requires comprehensive, precise and accurate characterization and monitoring.
TORONTO (PRWEB)
September 03, 2020
Join James Duffy, Assay Development Scientist, BioPharm CMC, Covance Inc. in a live webinar on Thursday, September 17, 2020 at 11am EDT (4pm BST) in which he will discuss the LC-MS approach to N-glycan characterization for a variety of biopharmaceutical products, as well as best practices for overcoming some of the most common product-related challenges.
N-glycosylation is a post-translational modification (PTM) that plays a crucial role in monoclonal antibody (mAb) effector functions and is, therefore, classified as a critical quality attribute (CQA) that requires comprehensive, precise and accurate characterization and monitoring.
N-glycosylation of mAbs (and other therapeutic proteins) has the potential to influence the pharmacodynamics (PD) and pharmacokinetic (PK) behavior, overall therapeutic efficacy and safety of the product because certain N-glycan species can cause adverse immune reactions, even at very low abundances. Therefore, a highly sensitive assay that can identify and quantify glycan species below 0.1 percent relative abundance is essential.
The webinar will provide:
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An introduction to glycosylation, typically observed N-glycan species and their importance as CQAs - An overview of platform LC-MS workflows for ‘first-look’ N-glycan profiling including intact mass, middle-up and peptide mapping analyses
- In-depth review of our current released N-glycan method using RapiFluor-MSTM labelling, with comparison to the traditional 2-AB technique
- An overview of the supplementary exoglycosidase linkage analysis used to provide additional confidence in N-glycan assignments and differentiate between isobaric species
- Focus on fusion proteins and products with additional N-glycan sites outside of the Fc-region with example data from our Aflibercept AMF, highlighting the challenges associated with analyzing more complex N-glycan profiles, as well as an overview of a specific digestion and separation strategy for assigning N-glycan profiles to discrete regions of the protein and further use of peptide map LC-MS analysis to identify site-specific glycan occupancy
For more information or to register for this event, visit N-Glycan Characterization via LC-MS.
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