Acylation of peptide hydroxyl groups with the Bolton-Hunter reagent

Brian T. Miller

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

Abstract

Reaction of the decapeptide gonadotropin releasing hormone (GnRH) with the Bolton-Hunter reagent produced a single major derivative. Mass spectrometric analysis of this derivative at M-Scan Corporation revealed that O-acylation of the Ser4 hydroxyl had occurred. Formation of the O-acylated Ser4 derivative was dependent on the presence of the His2 residue in GnRH. Similar experiments with several unrelated peptides revealed that the Bolton-Hunter reagent will readily acylate hydroxyl groups on serine, tyrosine, and threonine side chains located two positions from a histidine residue (e.g., His-X-Ser). Such O-acylated peptides can be formed under mild reaction conditions and appear to be relatively stable. Recognition of this sequence-specific O-acylation can be critical when labeling peptides with the Bolton-Hunter reagent and when interpreting experiments in which such modified peptides are used.

Original languageEnglish (US)
Pages (from-to)377-382
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume218
Issue number1
DOIs
StatePublished - Jan 5 1996
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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