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Glycosylation plays an important role in ensuring the proper structure and function of most biotherapeutic proteins. Even small changes in glycan composition, structure, or location can have a drastic impact on drug safety and efficacy. The AGRS works with biopharmaceutical companies as well as government regulatory agencies to create platforms for accurate and detailed analysis of biopharmaceutical protein glycosylation.

Research highlights:
  • Multi-level glycomic characterization of biotherapeutics from intact protein to native glycan
  • Isomer-specific structural characterization of N- and O-glycans
  • Comprehensive identification and quantitation of glycan modifications such as O-acetylation, polylactosaminylation, dehydration, phosphorylation, etc.
  • Screening of sample-specific non-human glycosylation.
  • Development a novel microfluidic chip for separation of sialylated and phosphorylated glycans
Relevant publications:
  • Seo, Y., Park, G.M., OH, M.J., An, H.J., “Investigation of O-glycosylation Heterogeneity of Recombinant Coagulation Factor IX using LC/MS/MS ”, Bioanalysis , 2017, 9(18)
  • Kim, U., OH, M.J., Seo, Y., Jeon, Y., Eom, J.H., An, H.J., “Sensitive and Comprehensive Analysis of O-glycosylation in Biotherapeutics: A Case Study of NESP”, Bioanalysis , 2017, 9(18)
  • OH, M.J., Hua, S., Kim, U., Kim, H.J., Lee, J., Kim, J.H., An, H.J., “Analytical detection and characterization of biopharmaceutical glycosylation by MS”, Bioanalysis , 2016, 8(7)
  • Hua S., Oh M.J., Ozcan S., Seo Y., Grimm R., An H.J., “Technologies for glycomic characterization of biopharmaceutical erythropoietins”, TrAC Trends in Analytical Chemistry, 2015, 68:18-27
  • Seo Y.. Kim U., Oh M.J., Yun N., An, H.J., “MS Platform for Erythropoietin Glycome Characterization.” Mass Spectrometry Letters, 2015, 6(3):53-58.