Cited by 38Neuropeptides and Animal PhysiologyChemical Synthesis and AnalysisReceptor Mechanisms and Signaling

Structure and function in neuropeptides

Schwyzer, R.·1980·Proceedings of the Royal Society of London. Series B. Biological Sciences

Abstract

This report reviews some aspects of the organization of molecular information, structure-activity relations and receptor interactions of three members of a family of neuroactive and hormonal peptides, adrenocorticotrophin (ACTH), alpha-melanotrophin (alpha-MSH) and the enkephalins, as they are presently being investigated in the author's laboratory (in collaboration with H. W. Kosterlitz, D. Schulster and P. W. Schiller). It has been established that ACTH acts on two different steroidogenically responsive receptors in rat adrenocortical cells: one that stimulates steroidogenesis without cyclic AMP synthesis and one that induces cyclic AMP production. This finding is a further example of the pleiotropic action of the opiocortin gene through different mechanisms. Another recent discovery, also related to the organization of ACTH information, reveals an unexpected interaction of ACTH(1-24) with lipid bilayer membranes: the molecule binds to the membranes in a reversible fashion and penetrates them. Parts of the hormonal message are exposed on the side of the membrane opposite to that to which the hormone was added. New 'fat' amino acids like carboranylalanine and adamantylalanine, as well as t-butylglycine, have been used to establish structure-activity relations and the influence of strongly enhanced lipophilicity on the biological activity of the enkephalins. An address/potentiator function of the two C-terminal amino acids is suggested. Tobacco mosaic virus (TMV) has been used as a carrier for covalently attached peptide hormones. Attachment of large numbers of hormone molecules endows these conjugates with the properties of superpotency, superaffinity and prolonged action on the target cell. Some of these properties are illustrated by TMV-enkephalin conjugates.

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Registry

Crossref · 10.1098/rspb.1980.0115

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31 of 31 references verified0 citation errors · 0 not checkable

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  • The most N-terminal region (Ser-Tyr-Ser) has been reported to potentiate the action of the HFRW sequence.

    “The most N-terminal region (Ser–Tyr–Ser) has been reported to potentiate the action of the HFRW sequence (46).”

    From ACTH Antagonists (2016) · cites this paper as [46]

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Authors
Schwyzer, R.
Affiliations
ETH Zurich (CH)
Corresponding author
Schwyzer, R.
Venue
Proceedings of the Royal Society of London. Series B. Biological Sciences
Published
1980-10-29
Volume
210
Issue
1178
Pages
5-20
ISSN
  • 0080-4649 (ISSN-L)
  • 2053-9193
OpenAlex
W2018317190
Cited by
38
References
31
Citations by year
2024: 1 · 2021: 1 · 2020: 1 · 2016: 1 · 2015: 1 · 2013: 2
FWCI
1.30
Type
journal article
Language
en
Open access
closed
Locations
  • Proceedings of the Royal Society B Biological Sciences (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuropeptides and Animal Physiology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Keywords
neuropeptides, ACTH, enkephalin, structure-activity relationship, cyclic AMP, adrenocortical cells, membrane binding, lipophilicity, C-terminal amino acids, tobacco mosaic virus, peptide conjugates
MeSH terms
Adrenocorticotropic Hormone, Amino Acid Sequence, Binding Sites, Biological Transport, Endorphins, Enkephalins, Lipid Bilayers, Melanocyte-Stimulating Hormones, Peptide Fragments, Receptors, Cell Surface, Solubility, Structure-Activity Relationship, Tobacco Mosaic Virus

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