2. Academic Validation
  3. "Tag and Modify" Protein Conjugation with Dynamic Covalent Chemistry

"Tag and Modify" Protein Conjugation with Dynamic Covalent Chemistry

  • Bioconjug Chem. 2018 Aug 15;29(8):2665-2670. doi: 10.1021/acs.bioconjchem.8b00358.
Maksymilian Marek Zegota 1 2,  Tao Wang 2 3,  Christiane Seidler 1 2,  David Yuen Wah Ng 1 2,  Seah Ling Kuan 1 2,  Tanja Weil 1 2
Affiliations

Affiliations

  • 1 Max-Planck Institute for Polymer Research , Ackermannweg 10 , 55128 Mainz , Germany.
  • 2 Institute of Inorganic Chemistry I , University of Ulm , Albert-Einstein-Allee 11 , 89081 Ulm , Germany.
  • 3 School of Materials Science and Engineering , Southwest Jiaotong University , 610031 Chengdu , P.R. China.
PMID: 29949347 DOI: 10.1021/acs.bioconjchem.8b00358
Abstract

The development of small protein tags that exhibit bioorthogonality, bond stability, and reversibility, as well as biocompatibility, holds great promise for applications in cellular environments enabling controlled drug delivery or for the construction of dynamic protein complexes in biological environments. Herein, we report the first application of dynamic covalent chemistry both for purification and for reversible assembly of protein conjugates using interactions of boronic acid with diols and salicylhydroxamates. Incorporation of the boronic acid (BA) tag was performed in a site-selective fashion by applying disulfide rebridging strategy. As an example, a model protein Enzyme (lysozyme) was modified with the BA tag and purified using carbohydrate-based column chromatography. Subsequent dynamic covalent "click-like" bioconjugation with a salicylhydroxamate modified Fluorescent Dye (BODIPY FL) was accomplished while retaining its original enzymatic activity.

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