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.
Zheng et al. (Mon,) studied this question.