Site-Specific Glycoconjugation of Protein via Bioorthogonal Tetrazine Cycloaddition with a Genetically Encoded trans-Cyclooctene or Bicyclononyne | Zendy

Takuya Machida | Zendy; Kathrin Lang | Zendy; Lin Xue | Zendy; Jason W. Chin | Zendy; Nicolas Winssinger | Zendy

Open Access

Site-Specific Glycoconjugation of Protein via Bioorthogonal Tetrazine Cycloaddition with a Genetically Encoded trans-Cyclooctene or Bicyclononyne

Author(s) -

Takuya Machida,

Kathrin Lang,

Lin Xue,

Jason W. Chin,

Nicolas Winssinger

Publication year - 2015

Publication title -

bioconjugate chemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.279

H-Index - 172

eISSN - 1520-4812

pISSN - 1043-1802

DOI - 10.1021/acs.bioconjchem.5b00101

Subject(s) - tetrazine , bioorthogonal chemistry , chemistry , cyclooctene , cycloaddition , azide , glycan , bioconjugation , alkyne , biochemistry , combinatorial chemistry , click chemistry , glycoprotein , organic chemistry , catalysis

Efficient access to proteins modified site-specifically with glycans is important in glycobiology and for therapeutic applications. Herein, we report a biocompatible protein glycoconjugation by inverse demand Diels-Alder reaction between tetrazine and trans-cyclooctene. Tetrazine functionalized glycans were obtained in one step by CuAAC (Cu-catalyzed alkyne azide cycloaddition) between glycosyl azide and an alkyne-tetrazine adduct. Site-specific glycoconjugation was performed chemoselectively on a target protein in which a trans-cyclooctene derivatized lysine was genetically encoded. Glycoconjugation proceeded to completion on purified protein and was shown to be selective for the target protein in E. coli.

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