원문정보
초록
영어
Therapeutic proteins play an increasingly important role in the pharmaceutical industry. Glycosylation is a very critical modification of therapeutic proteins, known to significantly modulate yield, bioactivity, solubility, immunogenicity and efficacy. Most biotherapeutic proteins developed to date have been produced using the mammalian model. Although mammalian system can produce glycosylation similar to human, they also produce non-human glycosylation that can cause immune responses and safety issue. Firstly, we explored difference of glycosylation between human and mouse to design glycan-humanized mouse model. We selectively enriched glycans from blood cell (red blood cell and white blood cell) membrane and analyzed them by porous graphitized carbon (PGC) based nano-LC/MS which enables to confirm not only glycan composition but also structure isomer. Hundreds of glycan structures were directly detected by accurate mass and structurally elucidated by MS/MS, revealing the species-specific structure. These results could be targets for new signatures distinguishing the species and the beginning for design of glycan-humanized mouse model.