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Updated: Sep 19, 2025

Genetic Encoding of a Non-Canonical Amino Acid for the Generation of Antibody-Drug Conjugates Through a Fast Bioorthogonal Reaction

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Tuning Encodable Tetrazine Chemistry for Site-Specific Protein Bioorthogonal Ligations.

Subhashis Jana, Alex J Eddins, Yogesh M Gangarde

Biorxiv : the Preprint Server for Biology

|June 6, 2025

Summary

Researchers developed new tetrazine amino acids for bioorthogonal chemistry, enabling faster and more stable protein labeling within cells using genetic code expansion. This enhances tools for site-specific protein modification.

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Area of Science:

Biochemistry
Chemical Biology
Molecular Biology

Background:

Genetic code expansion (GCE) enables bioorthogonal chemistry for protein labeling.
Tetrazine amino acids offer tunable properties for bioorthogonal ligations.

Purpose of the Study:

To synthesize and characterize novel tetrazine amino acids for enhanced protein labeling.
To develop the most stable and reactive tetrazine system for in-cell applications.

Main Methods:

Synthesis and kinetic characterization of 29 tetrazine amino acids.
Evaluation of Tet ncAA encoding efficiency using tRNA/RS pairs.
Assessment of on-protein stability, reactivity, and in-cell labeling.

Main Results:

Identified 20 new tetrazine amino acids with tunable properties.
Developed a highly stable and reactive Tet system (Tet4 with fluorine substituents).
Achieved reaction rates of 10⁶ M⁻¹s⁻¹ for Tet-sTCO ligations.

Conclusions:

Tetrazine amino acids are highly tunable and potent bioorthogonal functional groups.
The developed Tet system represents a significant advancement in site-specific protein labeling.
Findings provide a basis for further exploration of Tet-ncAA encoding and reactivity.