Glyco-modification of Protein with O-cyanate Chain-end Functionalized Glycopolymer via Isourea Bond Formation

Valentinas Gruzdys; Hailong Zhang; Xue-Long Sun

doi:10.1080/07328303.2014.922189

Glyco-modification of Protein with O-cyanate Chain-end Functionalized Glycopolymer via Isourea Bond Formation

Valentinas Gruzdys, Hailong Zhang, Xue-Long Sun

Cleveland State University

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	American English
Journal	Journal of Carbohydrate Chemistry
Volume	33
DOIs	https://doi.org/10.1080/07328303.2014.922189
State	Published - Jan 1 2014

Keywords

Carbohydrate
glycopolymer
protein
thrombomodulin
cyanate
isourea

Disciplines

Chemistry
Medicinal-Pharmaceutical Chemistry

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10.1080/07328303.2014.922189License: CC BY

Glyco-modification of Protein with O-cyanate Chain-end FunctionalFinal published version, 1.05 MBLicense: CC BY

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title = "Glyco-modification of Protein with O-cyanate Chain-end Functionalized Glycopolymer via Isourea Bond Formation",

abstract = " 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.",

keywords = "Carbohydrate, glycopolymer, protein, thrombomodulin, cyanate, isourea",

author = "Valentinas Gruzdys and Hailong Zhang and Xue-Long Sun",

note = "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.",

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doi = "10.1080/07328303.2014.922189",

language = "American English",

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T1 - Glyco-modification of Protein with O-cyanate Chain-end Functionalized Glycopolymer via Isourea Bond Formation

AU - Gruzdys, Valentinas

AU - Zhang, Hailong

AU - Sun, Xue-Long

N1 - 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.

PY - 2014/1/1

Y1 - 2014/1/1

N2 - 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.

AB - 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.

KW - Carbohydrate

KW - glycopolymer

KW - protein

KW - thrombomodulin

KW - cyanate

KW - isourea

UR - https://engagedscholarship.csuohio.edu/scichem_facpub/507

U2 - 10.1080/07328303.2014.922189

DO - 10.1080/07328303.2014.922189

M3 - Article

VL - 33

JO - Journal of Carbohydrate Chemistry

JF - Journal of Carbohydrate Chemistry

ER -

Glyco-modification of Protein with O-cyanate Chain-end Functionalized Glycopolymer via Isourea Bond Formation

Abstract

Keywords

Disciplines

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