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Cation-induced conformational change in glucagon

R M Epand

    Molecular Pharmacology
    |July 1, 1982
    PubMed
    Summary

    Glucagon binds to terbium, significantly enhancing its fluorescence. This interaction, dependent on pH and histidine protonation, reveals glucagon

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    Area of Science:

    • Biochemistry
    • Spectroscopy
    • Protein Chemistry

    Background:

    • Glucagon is a peptide hormone with critical roles in glucose metabolism.
    • Understanding protein-metal ion interactions is key to elucidating biological mechanisms.
    • Fluorescence spectroscopy offers sensitive detection of molecular changes.

    Purpose of the Study:

    • To investigate the interaction between glucagon and terbium ions.
    • To characterize the influence of pH and metal ions on glucagon conformation.
    • To explore the potential of terbium fluorescence as a probe for glucagon.

    Main Methods:

    • Fluorescence spectroscopy was used to monitor terbium emission.
    • Experiments were conducted across a range of pH values.
    • Metal ion displacement assays (zinc, calcium) were performed.

    Main Results:

    • Terbium fluorescence was enhanced 1000-fold upon binding to glucagon.
    • Binding is pH-dependent, requiring an unprotonated N-terminal histidine.
    • Zinc ions displaced terbium, inducing significant conformational changes in glucagon, including increased helix content and a fluorescence emission shift.

    Conclusions:

    • Terbium is a sensitive fluorescent probe for glucagon.
    • Glucagon undergoes substantial conformational changes upon metal binding, influenced by pH.
    • These findings provide insights into glucagon's structural dynamics and metal ion interactions.

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