Abstract
Modification of amino acids is an important strategy in organic and bioorganic chemistry. In contrast to common side-chain functionalization, backbone modification is much less explored.
Especially glycine units seem to be attractive and versatile since a wide range of functionality can be potentially introduced. We report here oxidative modification of glycinates that are stable and enable further functionalization.
Selective glycinate enolate oxidation by TEMPO or a FeCp(2)PF(6)/TEMPO reagent combination provides stable alkoxyamines in good to excellent yields. The methodology is expanded to glycine-containing dipeptides demonstrating selective oxygenation at the glycine unit.
The orthogonal reactivity potential of oxygenated glycines for transformation to other amino acid derivatives is explored.