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Structure-Activity Relationships of Arodyn, a Novel Dynorphin A-(1–11) Analogue
Book chapter

Structure-Activity Relationships of Arodyn, a Novel Dynorphin A-(1–11) Analogue

Marco A. Bennett, Thomas F. Murray and Jane V. Aldrich
Peptides: The Wave of the Future, pp.894-895
American Peptide Symposia, Springer Netherlands
2001

Abstract

Drug Alcohol Depend Endogenous Agonist Kappa Opioid Receptor Opioid Receptor Radioligand Binding Assay
The opioid receptors, mu (μ), kappa (κ) and delta (δ), are widely distributed throughout the peripheral and central nervous system. When activated, the opioid receptors attenuate the transmission of pain signals to the spinal cord. Dynorphin A, an endogenous agonist at κ receptors, shares a common N-terminal “message” sequence (Tyr-Gly-Gly-Phe) with most mammalian opioid peptides and has a unique C-terrninal “address” sequence [1]. The “message” sequence has been reported to be important for k activation, while the “address” sequence is designated as the potency-enhancing domain [1].

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