ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2025
Bioorthogonal Reaction of o-Quinone with Furan-2(3H)-One for Site-Selective Tyrosine Conjugation and Construction of Bispecific Antibody Complexes.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Advancements and applications of click chemistry in protein labeling and bioconjugation.RSC advances · 2026Review
- The evolving landscape of enzymatic technologies for precision synthesis of antibody-drug conjugates.Antibody therapeutics · 2026Review
- Bioorthogonal Reaction of o-Quinone with Furan-2(3H)-One for Site-Selective Tyrosine Conjugation and Construction of Bispecific Antibody Complexes.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
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14 authors.
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Abstract
Bioorthogonal reactions enable the chemical conjugation of functional moieties to native proteins and empower the development of new diagnostic tools and therapeutics. Through site-selective reactions, therapeutic molecules can be conjugated with antibodies in a stoichiometry- and site-controlled manner. Here, a one-pot chemoenzymatic reaction is reported that preferentially modifies a terminal tyrosine of recombinant proteins, or tyrosine 296 in the Fc domain of selected human antibodies. This reaction combines tyrosinase-catalyzed oxidation of phenol to o-quinone, the bioorthogonal addition reaction of o-quinone with an azide-containing furan-2(3H)-one (FuA) moiety, and the subsequent azide click reactions. To this surprise, experimental evidence indicates that the o-quinone-FuA reaction proceeds through nucleophilic addition instead of the cycloaddition pathway. This reaction enables site-selective modification of therapeutic human antibodies, including atezolizumab, trastuzumab, daratumumab, and cetuximab. Monofunctionalized antibody conjugates and DNA-templated bispecific antibody complexes (DNA-bsAbC) are thus constructed in a modular way. DNA-bsAbC acts as a bispecific engager to mediate the interaction between immune cells and cancer cells, resulting in antibody-dependent cellular cytotoxicity (ADCC) toward cancer cells. Taken together, here a bioorthogonal reaction is reported for site-selective tyrosine conjugation in recombinant proteins and human antibodies and showcase its application in constructing antibody conjugates for potential applications in immunotherapies.
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