Glycine-selective α-carbon-nitrogen bond cleavage of dipeptides by nickel peroxide

Nickel peroxide selectively cleaves the α-carbon-nitrogen bond of glycine residues in dipeptide derivatives to give the corresponding amides. The glycine selectivity is attributable to preferential complexation of the reactant residue to nickel peroxide and subsequent reaction via a stable α-centred...

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Bibliographic Details
Published in:Tetrahedron 1997-04, Vol.53 (15), p.5609-5616
Main Authors: Easton, Christopher J., Eichinger, Sharon K., Pitt, Michael J.
Format: Article
Language:English
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Summary:Nickel peroxide selectively cleaves the α-carbon-nitrogen bond of glycine residues in dipeptide derivatives to give the corresponding amides. The glycine selectivity is attributable to preferential complexation of the reactant residue to nickel peroxide and subsequent reaction via a stable α-centred glycyl radical. The oxidation process serves as a chemical model for peptidylglycine α-amidating monooxygenase (PAM) and, in addition, may have potential for the synthesis of α,β-didehydro amino acid residues within peptides. Nickel peroxide selectively cleaves glycine residues in dipeptides to give the corresponding amides, in a process analogous to that catalysed by peptidylglycine α-amidating monooxygenase (PAM).
ISSN:0040-4020
1464-5416
DOI:10.1016/S0040-4020(97)00216-0