Akademik Veri Yönetim Sistemi
ANALYTICAL LETTERS, 2024 (SCI-Expanded)
Monoclonal antibodies (mAbs) have become prevalent in the pharmaceutical sector for treating various diseases and have a significant market presence. The determination of these molecules is complex and challenging. It is necessary to employ high-throughput technologies to characterize these pharmaceuticals in order to characterize sequencing, structure, composition, conformation, and mass. It is important to perform an N-glycosylation study on these macromolecules as their N-glycan profiles have a significant impact on their effectiveness. However, the conformational features of the N-glycans on mAb are not adequately addressed in commonly used methods. This study incorporated ion-mobility mass spectrometry as an additional dimension to established hydrophilic liquid chromatography trapped ion mobility spectrometry with fluorescence detection ((HILIC)LC/TIMS/FLD) in order to enhance the characterization of N-glycan structures. The N-glycans derived from two distinct mAbs and an immunoglobulin G (IgG) protein were labeled with procainamide and determined by (HILIC)LC/FLD with TIMS. The N-glycan profiles obtained from mAbs and IgG were examined in terms of conformation. The alterations in the N-glycan conformations were ascertained with the insertion of distinct monosaccharide units, such as galactose, into the structure. This method can be employed to clarify the intricate structures of N-glycans and offer insights into the conformational features of monoclonal antibodies throughout their production.