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| Type |
Oral Presentation |
| Area |
Oral Presentation of Young Analytical Chemists Ⅰ |
| Room No. |
303호 |
| Time |
THU 10:14-: |
| Code |
ANAL1.O-30 |
| Subject |
Assessing Biosimilarity of Therapeutic Glycoprotein using Intact Glycopeptide |
| Authors |
서영숙, 안현주*
충남대학교 분석과학기술대학원, Korea
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| Abstract |
Therapeutic glycoprotein exhibits structural heterogeneity and complexity due to co-occurred glycans on a protein. Drug’s glycosylation has enormous effect on biological activity, immunogeneicity, and serum half-life. Therefore, glycomic characterization is of great importance to prove drug’s quality. With the increase of biosimilars, analytical tools for glycan profiling have been developed to evaluate the compatibility with the reference drug in efficacy and safety. Here, we present an analytical strategy to determine glycosylation similarity of therapeutic glycoproteins using intact glycopeptide. As a proof of concept, we selected recombinant erythropoietins (rhEPOs) having multiple glycosylation sites and glycan variants. The rhEPO was treated using specific protease, trypsin, to obtain glycopeptides having sugar moieties with peptide tag. We determined two intact glycopeptides of rhEPO in LC/MS analysis. One is major glycopeptide containing two N-glycosylation sites (83Asn and 88Asn), which indicates a distinctive glycosylation pattern with different O-acetylation on NeuAc. The other glycopeptide having three N-glycosylation sites (38Asn, 30Asn, and 25Asn) was also identified by glycan correlation. Using intact glycopeptide analysis, we could rapidly screen the glycoform distribution of rhEPOs for assessing biosimilarity. |
| E-mail |
ysseo910@gmail.com |
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119th General Meeting of the KCS