Characterization of Monoclonal Antibody N-Glycan Conformations by Novel Hydrophilic Interaction Liquid Chromatography (HILIC) with Trapped Ion Mobility Mass Spectrometry (TIMS) and Fluorescence Detection (FLD)
Yazarlar (4)
Izzet Avci
Hacettepe Üniversitesi, Türkiye
Mehmet Atakay Hacettepe Üniversitesi, Türkiye
Doç. Dr. Hacı Mehmet KAYILI Karabük Üniversitesi, Türkiye
Bekir Salih Hacettepe Üniversitesi, Türkiye
Makale Türü Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale)
Dergi Adı Analytical Letters (Q3)
Dergi ISSN 0003-2719 Wos Dergi Scopus Dergi
Dergi Tarandığı Indeksler SCI-Expanded
Makale Dili Türkçe Basım Tarihi 07-2025
Cilt / Sayı / Sayfa 58 / 12 / 2158–2173 DOI 10.1080/00032719.2024.2384700
Makale Linki https://doi.org/10.1080/00032719.2024.2384700
UAK Araştırma Alanları
Analitik Kimya
Özet
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 …
Anahtar Kelimeler
High-performance liquid chromatography (HPLC) | hydrophilic interaction liquid chromatography with fluorescence detection (HILIC-FLD) | monoclonal antibodies | N-glycan | trapped ion-mobility mass spectrometry (TIMS)