Protein modification enables the study and modulation of cellular events in which proteins play important roles. Our lab focuses on developing new bioorthogonal reactions for the site-specific protein conjugations, combining with approaches that conveniently accessible to biological labs. Base on our previous investigations, we have designed and synthesized several peptides or unnatural amino acids that allow the incorporation of desired functionalities to the C-terminus of proteins through different chemoenzymatic methods or unnatural amino acid mutagenesis. These site-specific protein functionalities subsequently react with complementary probes with a fast speed, forming tricyclic boron-nitrogen heterocycles that are stable at physiological and acidic pHs.<br/>In this work, we present the synthesis of a new unnatural amino acid that potentially can be attached to C-terminal protein through enzyme-mediated ligation. Model reactions with this unnatural amino acid were examined and characterized, including kinetics profiles and stability of the products at various pHs. The accessibility of attaching this unnatural amino acid to proteins through enzymatic methods will be presented. The reactivity and stability of the functionalized protein conjugation will be also discussed.

New bioorthogonal approaches for C-terminal protein modification

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.