Chemical Modification of Peptides Containing γ-Carboxyglutamic Acid

Norman T. Boggs, H. David Bruton, Daniel H. Craig, Joseph A. Helpern, Henry C. Marsh, Mark D. Pegram, David J. Vandenbergh, Karl A. Koehler, Richard G. Hiskey

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

At acidic pH the γ-proton of the γ-carboxyglutamic acid (Gla) side chain undergoes rapid exchange. We have utilized the reactivity of the resulting enol form to develop a method for the chemical modification of peptide-bound Gla residues. Reaction of Gla peptides with a morpholine-formaldehyde mixture at pH 4.5 yields the Mannich base adduct. Fragmentation of the Mannich base occurs rapidly in 50% aqueous DMF to yield carbon dioxide, morpholine, and the corresponding γ-methyleneglutamyl residue.

Original languageEnglish (US)
Pages (from-to)1812-1816
Number of pages5
JournalJournal of Organic Chemistry
Volume47
Issue number10
DOIs
StatePublished - 1982

All Science Journal Classification (ASJC) codes

  • Organic Chemistry

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