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Journal of Carbohydrate Chemistry Volume 33, 2014 - Issue 7-8: Advances in Carbohydrate Chemistry and Glycobiology
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Original Articles

Glyco-Modification of Protein With O-Cyanate Chain-End Functionalized Glycopolymer via Isourea Bond Formation

Valentinas GruzdysDepartment of Chemistry, Chemical and Biomedical Engineering, and Center for Gene Regulation in Health and Disease (GRHD), Cleveland State University, Cleveland, OH44115, USA
,
Hailong ZhangDepartment of Chemistry, Chemical and Biomedical Engineering, and Center for Gene Regulation in Health and Disease (GRHD), Cleveland State University, Cleveland, OH44115, USA
&
Xue-Long SunDepartment of Chemistry, Chemical and Biomedical Engineering, and Center for Gene Regulation in Health and Disease (GRHD), Cleveland State University, Cleveland, OH44115, USACorrespondence[email protected]
Pages 368-380 | Received 29 Mar 2014, Accepted 05 May 2014, Published online: 12 Jun 2014
 
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Abstract

Glycoengineering aimed at the addition of carbohydrates to proteins is an attractive approach to alter the 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 with activity from the glycopolymer modification. The isourea bond formation under mild conditions was demonstrated as an alternative method for protein modification with polymers.

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