Cited by 883Neuropeptides and Animal PhysiologyNeuroendocrine regulation and behaviorChemical Synthesis and Analysis

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Dynorphin-(1-13), an extraordinarily potent opioid peptide.

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Goldstein, A, Tachibana, S, Lowney, L I, Hunkapiller, M, Hood, L·1979·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.76.12.6666PMC PMC411929

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Abstract

We describe the opioid properties of a tridecapeptide, the sequence of which corresponds to the NH2-terminal sequence of dynorphin, a novel porcine pituitary endorphin. It contains [Leu]enkephalin. In the guinea pig ileum longitudinal muscle preparation it is about 700 times more potent than [Leu]enkephalin. Its effects in this tissue are blocked completely by naloxone, but the apparent affinity of naloxone is 1/13th that for blockade of [Leu]enkephalin or normorphine. In the mouse vas deferens, this peptide is 3 times more potent than [Leu]enkephalin. Well-washed rat brain membranes degrade the peptide rapidly, suggesting the presence of a membrane-bound degradative enzyme. The peptide displays considerable immunoreactivity in assays with antisera that have been used for the immunohistochemical localization of [Leu]enkephalin. The remarkable enhancement of the potency of [Leu]enkephalin by the COOH-terminal extension -Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-OH suggests new interpretations concerning the structure of opiate receptors and the function of the enkephalin pentapeptides.

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“Intriguingly, dynorphin displayed similar potency to ethylketo-cyclazocine, a synthetic KOR agonist, leading to the hypothesis that dynorphins are the endogenous KOR ligand [103].”

Authors: Goldstein, A., Tachibana, S., Lowney, L. I., Hunkapiller, M., & Hood, L.
Affiliations: California Institute of Technology (US)
ORCID: Hunkapiller, M
Hood, L
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1979-12
Volume: 76
Issue: 12
Pages: 6666-6670
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.76.12.6666
PMC: PMC411929
OpenAlex: W2033680879
Cited by: 882
References: 18
Citations by year: 2026: 8 · 2025: 9 · 2024: 8 · 2023: 14 · 2022: 10 · 2021: 14 · 2020: 23 · 2019: 13 · 2018: 8 · 2017: 9 · 2016: 6 · 2015: 8 · 2014: 16 · 2013: 23 · 2012: 18
FWCI: 24.93
Type: journal article
Language: en
Open access: green
europepmc.org
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
CaltechAUTHORS (California Institute of Technology) (submittedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuropeptides and Animal Physiology
Life Sciences › Neuroscience › Endocrine and Autonomic Systems › Neuroendocrine regulation and behavior
Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
Keywords: dynorphin A(1-13), opioid peptides, leu-enkephalin, enkephalin, naloxone, opioid receptors, vas deferens, peptide degradation, immunoreactivity
MeSH terms: Amino Acid Sequence, Animals, Biological Assay, Dose-Response Relationship, Drug, Endorphins, Guinea Pigs, Ileum, Radioligand Assay, Receptors, Opioid, Structure-Activity Relationship, Swine, Rats

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Dynorphin-(1-13), an extraordinarily potent opioid peptide.

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