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Chemical modification of a specific amino acid residue on peptides represents an efficient strategy to improve their pharmacokinetics and facilitates the potential to achieve post-synthetic diversification of peptides. Herein, we reported the first Pd-catalyzed late-stage ortho -olefination of Tyr residues on peptides with high chemo- and site-selectivity, by employing the easily attached and removable silanol as a bifunctional protecting group and directing group. Up to hexapeptides with variation on amino acid sequences or locations of the Tyr residue and different olefins were compatible with this protocol, which enriched the chemical toolbox for late-stage modification via C(sp 2 )-H functionalization. Furthermore, the orthogonal protection strategies of Tyr were also developed and could be applied to SPPS., Competing Interests: The authors declare no conflict of interest., (This journal is © The Royal Society of Chemistry.)