Among hydrazide nucleophiles, azaglycine derivatives constitute a unique class (Scheme 1C). These amino acid analogs, in which the α-carbon is replaced by a nitrogen atom, enable the fine-tuning of the structural and conformational features of bioactive peptides. Notably, azapeptides exhibit enhanced protease stability, 5 greater H-bonding capability, and usually favor β-turn. While N-alkylation and N-arylation of azaglycine have been reported, to the best of our knowledge, N-alkynylation remains unexplored. Moreover, α-alkynyl amino acids have been shown to be irreversible enzyme inhibitors and versatile building blocks in the synthesis of bioactive compounds. An easy access to their α-alkynyl azaglycine analogues would therefore be valuable. Scheme 1. (A) Alkynylation of nitrogen-based nucleophiles, (B) Current method to access ynehydrazides, (C) Towards -alkynyl azaglycine derivatives, (D) Our work.