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Structure and function in neuropeptides.

R Schwyzer

    Proceedings of the Royal Society of London. Series B, Biological Sciences
    |October 29, 1980
    PubMed
    Summary
    This summary is machine-generated.

    This study explores adrenocorticotrophin (ACTH) and enkephalins, revealing ACTH

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    Area of Science:

    • Neuroendocrinology
    • Molecular Pharmacology
    • Biochemistry

    Background:

    • Neuroactive and hormonal peptides, including adrenocorticotrophin (ACTH), alpha-melanotrophin (alpha-MSH), and enkephalins, play crucial roles in physiological processes.
    • Understanding the molecular organization, structure-activity relationships, and receptor interactions of these peptides is essential for elucidating their biological functions.
    • Previous research has indicated the pleiotropic actions of the opiocortin gene, suggesting diverse mechanisms of peptide hormone signaling.

    Purpose of the Study:

    • To investigate the dual receptor interactions of ACTH in rat adrenocortical cells.
    • To explore the interaction of ACTH(1-24) with lipid bilayer membranes.
    • To establish structure-activity relationships for enkephalins by incorporating lipophilic amino acids and to assess the potential of tobacco mosaic virus (TMV) as a carrier for peptide hormones.

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    Main Methods:

    • Characterization of ACTH receptor binding and downstream signaling pathways in rat adrenocortical cells.
    • Investigation of ACTH(1-24) membrane binding and penetration using biophysical techniques.
    • Synthesis and biological evaluation of modified enkephalins with enhanced lipophilicity and conjugation of peptide hormones to TMV.

    Main Results:

    • ACTH was found to interact with two distinct receptors in rat adrenocortical cells: one stimulating steroidogenesis independently of cyclic AMP, and another inducing cyclic AMP production.
    • ACTH(1-24) demonstrated reversible binding and penetration of lipid bilayer membranes, with parts of the hormonal message exposed on the opposite side.
    • Incorporation of lipophilic amino acids altered enkephalin biological activity, suggesting a role for enhanced lipophilicity. TMV-peptide hormone conjugates exhibited superpotency, superaffinity, and prolonged action.

    Conclusions:

    • ACTH exhibits pleiotropic actions through distinct receptor mechanisms, highlighting the complexity of opiocortin gene signaling.
    • The interaction of ACTH with lipid membranes suggests novel mechanisms for peptide hormone delivery and action.
    • TMV-based peptide hormone conjugates represent a promising strategy for developing superpotent and long-acting therapeutic agents.