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Updated: Sep 17, 2025

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

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

Published on: September 14, 2018

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

Ryan A Mehl¹, Subhashis Jana¹, Alex J Eddins¹

¹Department of Biochemistry and Biophysics and GCE4All Research Center, Oregon State University, Corvallis, Oregon, 97331, USA.

Angewandte Chemie (International Ed. in English)

|July 3, 2025

Summary

Researchers developed new tetrazine (Tet) amino acids for bioorthogonal chemistry, enabling faster and more stable protein labeling within cells. This advancement expands tools for site-specific protein modification.

Keywords:

Bioorthogonal ligation Genetic code expansion Inverse electron demand Diels–Alder reaction In‐cell labeling Tetrazine amino acid

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Last Updated: Sep 17, 2025

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Published on: August 19, 2012

Area of Science:

Biochemistry
Chemical Biology

Background:

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

Purpose of the Study:

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

Main Methods:

Developed and characterized 29 Tet amino acids, including 20 new ones.
Utilized evolved tRNA/RS pairs for encoding Tet amino acids into proteins.
Assessed on-protein stability, reaction kinetics, and ligation efficiency.

Main Results:

Identified highly tunable Tet amino acids with potential for fast, quantitative bioorthogonal ligations.
Engineered a novel Tet amino acid (Tet4 with fluorine substituents) exhibiting reaction rates of 10⁶ M⁻¹s⁻¹.
Achieved the smallest, fastest, and most stable Tet for in-cell protein labeling.

Conclusions:

Tet amino acids are a tunable, reactive, and encodable bioorthogonal functional group.
The developed Tet reagents significantly expand the toolbox for site-specific protein labeling.
This work lays the groundwork for further exploration of Tet encoding and reactivity.