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Glyco-modification of Protein with O-cyanate Chain-end Functionalized Glycopolymer via Isourea Bond Formation
Journal of Carbohydrate Chemistry
  • Valentinas Gruzdys, Cleveland State University
  • Hailong Zhang, Cleveland State University
  • Xue-Long Sun, Cleveland State University
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Glycoengineering aimed at addition of carbohydrates to proteins is an attractive approach to alter pharmacokinetic properties of proteins such as enhancing stability and prolonging the duration of action. We report a novel protein glyco-modification of BSA and recombinant thrombomodulin with O-cyanate chain-end functionalized glycopolymer via isourea bond formation. The protein glycoconjugates were confirmed by SDS-PAGE, western blot, and MALDI-TOF Mass Spectrometry. Protein C activation activity of the glyco-modified recombinant thrombomodulin was confirmed, proving no interference to activity from the glycopolymer modification. The isourea bond formation under mild conditions was demonstrated as an alternative method for protein modification with polymers.


This work was partly supported by grants from the NIH (1R01HL102604-04, X.-L. Sun), National Science Foundation MRI Grant (CHE-1126384, X.-L. Sun), Faculty Research Development Fund and the research fund at the Center for Gene Regulation in Health and Disease (GRHD) at Cleveland State University supported by Ohio Department of Development (ODOD). MALDI TOF data was supported by the National Science Foundation under Grant No. MRI-0821515 at Case Western Reserve University.

Citation Information
Gruzdys, V.; Zhang, H.; Sun, X. Glyco-modification of protein with O-cyanate chain-end functionalized glycopolymer via isourea bond formation. J. Carbohydr. Chem. 2014, 33, 368-380.