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  • 02월 19일 10시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제121회 대한화학회 학술발표회, 총회 및 기기전시회 안내 A Simultaneous Determination of Highly Acidic Glycans in Biotherapeutics using PGC-SPE and LC-MS/MS

등록일
2018년 2월 6일 11시 08분 23초
접수번호
6503
발표코드
ANAL1.O-6 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
목 10시 : 03분
발표형식
구두발표
발표분야
Analytical Chemistry - Oral Presentation of Young Analytical Chemists I
저자 및
공동저자
Youngsuk Seo, Hyun Joo An*
Graduate School of Analytical Science and Technology, Chungnam National University, Korea
Glycosylation of therapeutic glycoproteins influences on pharmacological functions including efficacy, safety, and biological activity. In a therapeutic enzyme, phosphorylated glycans play a significant role as the target signal to enter into the lysosome. Sialylated glycans are also an important bioactive glycan which can improve in vivo recovery of a therapeutic enzyme. Therefore, the in-depth analysis of bioactive glycans has been required to ensure product consistency with the increase of the biosimilars market. However, glycosylation characterization of a therapeutic enzyme is still challengeable because of an increased heterogeneity by phosphorylated glycosylation as a modified glycoform and an extended sialylation. Here, we present an analytical approach to readily determine phosphorylated glycans and sialylated glycans, individually using porous graphitized carbon (PGC)-solid phase extraction (SPE). We successfully fractionated them according to varying proportions of acetonitrile in water and acid, though both phosphorylated glycans and sialylated glycans showed a high acidity. Each eluent was analyzed by LC/MS and CID MS/MS to fully characterize glycan composition, detailed structure, and relative quantitation. We observed mannose-phosphate series consisting of Man 5 to Man 9 decorated with mono-or di-phosphate groups. Sialylation of a therapeutic enzyme was mainly composed of glycans having two NeuAc residues. Bioactive glycan analysis of an original therapeutic enzyme and biosimilar is being further performed to demonstrate our analytical platform as an assessment tool for glycosylation biosimilarity.

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