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Minigastrin; corrected structure and synthesis

R A Gregory, H J Tracy, J I Harris

    Hoppe-Seyler'S Zeitschrift Fur Physiologische Chemie
    |January 1, 1979
    PubMed
    Summary
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    Minigastrin is confirmed as the C-terminal tetradecapeptide amide of gastrin, not the tridecapeptide amide. This study details its synthesis and purification, confirming its full physiological activity.

    Area of Science:

    • Peptide Chemistry
    • Gastroenterology

    Background:

    • Gastrin is a key hormone regulating gastric acid secretion.
    • The exact structure of minigastrin, a biologically active fragment of gastrin, has been debated.

    Purpose of the Study:

    • To synthesize and characterize the C-terminal tetradecapeptide amide of gastrin (minigastrin).
    • To resolve the structural discrepancy regarding minigastrin's length.

    Main Methods:

    • Solid-phase peptide synthesis utilizing fragment coupling with dicyclohexylcarbodiimide and N-hydroxysuccinimide/1-hydroxybenzotriazole.
    • Purification of intermediates and final product using Sephadex LH-20 and ion-exchange chromatography.
    • Deprotection using 90% trifluoroacetic acid with scavengers.

    Main Results:

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    • Successful synthesis of the tetradecapeptide amide sequence: Trp-Leu-[Glu]5-Ala-Tyr-Gly-Trp-Met-Asp-Phe-NH2.
    • Purification yielded a homogeneous tetradecapeptide amide.
    • The synthesized minigastrin exhibited full physiological activity.

    Conclusions:

    • Minigastrin is definitively the C-terminal tetradecapeptide amide of gastrin.
    • The synthetic methodology provides a reliable route for producing active minigastrin.