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  • Advanced assessment through intact glycopeptide analysis of Infliximab's biologics and biosimilar.

Advanced assessment through intact glycopeptide analysis of Infliximab's biologics and biosimilar.

Frontiers in molecular biosciences (2022-12-17)
Hyejin Kim, Geul Bang, Ye Eun Park, Moonhee Park, Jung Hoon Choi, Myung Jin Oh, Hyun Joo An, Jong Shin Yoo, Youngja Hwang Park, Jin Young Kim, Heeyoun Hwang
ABSTRACT

Characterization of therapeutic monoclonal antibodies (mAbs) represents a major challenge for analytical sciences due to their heterogeneity associated with post-translational modifications (PTMs). The protein glycosylation requires comprehensive identification, which could influence on the mAbs' structure and their function. Here, we demonstrated high-resolution tandem mass spectrometry with an ultra-high-performance liquid chromatography for characterization and comparison between biologics and biosimilar of infliximab at an advanced level. Comparing the N- and O-glycopeptides profiles, a total of 49 and 54 glycopeptides was identified for each product of the biologics and biosimilar, respectively. We also discovered one novel N-glycosylation site at the light chain from both biopharmaceuticals and one novel O-glycopeptide at the heavy chain from only biosimilar. Site-specific glycopeptide analysis process will be a robust and useful technique for evaluating therapeutic mAbs and complex glycoprotein products.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
SILuMAb Infliximab Stable-Isotope Labeled Monoclonal Antibody, recombinant, expressed in CHO cells