Acylation of peptide hydroxyl groups with the Bolton-Hunter reagent

Brian T. Miller

    Research output: Contribution to journalArticle

    14 Citations (Scopus)

    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

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    Acylation
    Hydroxyl Radical
    Peptides
    Derivatives
    Gonadotropin-Releasing Hormone
    Threonine
    Histidine
    Labeling
    Serine
    Tyrosine
    Experiments
    Bolton-Hunter reagent
    Industry

    ASJC Scopus subject areas

    • Biochemistry
    • Biophysics
    • Molecular Biology

    Cite this

    Acylation of peptide hydroxyl groups with the Bolton-Hunter reagent. / Miller, Brian T.

    In: Biochemical and Biophysical Research Communications, Vol. 218, No. 1, 05.01.1996, p. 377-382.

    Research output: Contribution to journalArticle

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