A Catalyst-Free, Tyrosine-Selective Bioconjugation Strategy via Triazine-Pyridine Chemistry for Antibodies

Organic Letters 2026

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Authors: Shanyue Zheng, C. Y. Wang, Yifan Wang, Ruijuan Yin, Rilei Yu, Lu Liu, Hao Jiang, Xuechen Li, Tao Jiang
DOI: 10.1021/acs.orglett.6c00680
Cited by: 2
References: 29

Abstract

A catalyst-free, tyrosine-selective bioconjugation strategy was successfully developed by utilizing triazine-pyridine chemistry. This approach employs 1,3,5-triazine–pyridinium probes to achieve efficient and selective modification of tyrosine (Tyr) residues in peptides and antibodies under physiological conditions. The optimized probe 2b, which exhibits excellent selectivity and reactivity (yield >95%), labeled antibodies such as trastuzumab at Tyr, while maintaining antibody integrity and antigen-binding activity. The utility of this method was demonstrated by the generation of biologically relevant antibody conjugates, highlighting its potential for antibody–drug conjugate (ADC) development.

Fields of Study & Subjects

Click Chemistry and Applications Synthesis and Characterization of Heterocyclic Compounds Synthesis and biological activity

Publication details

Journal / source
Organic Letters
Publisher
American Chemical Society (ACS)
Volume
28
Issue
12
Pages
3862–3868
Publication date
16 March 2026
Language
EN