원문정보
초록
영어
More than 60% of protein therapeutics are glycoproteins attached with glycans which play crucial roles for folding, therapeutic efficacy, in vivo half-life and immunogenecity. Therefore, the analysis of their glycan structures is of great importance especially when developing glycoprotein therapeutics and remodeling glycosylation pathway for improved expression hosts [1]. We builded up the glycan analysis system based on high performance liquid chromatography (HPLC), matrix-assisted laser desorption/ionization tim e-of-flight m ass spectrometry (MALDI-TOF MS) and DNA sequencer. It was nicely able to characterize and monitor the glycosylation patterns of protein therapeutics including three representative categories (cytokines, therapeutic antibody and enzyme). Glycan profile of HPLC provided quantitative information robustly and reproducibly for each peak of glycan while MALDI-TOF could be successfully employed for the identification of glycan structures. On the other hand, DNA sequencebased methods could generate quantitative information for glycan profiling in a high-throghput manner using 96-well formats [2], which allows rapid and efficient screening for glycoegnineerng and glycan remodeling.