Peptides: The Wave of the Future pp 689-690 | Cite as
C-Terminal Structure-Activity Relationships for the Novel Opioid Peptide JVA-901 (Venorphin)
Chapter
Abstract
We previously reported a novel kappa opioid receptor antagonist JVA 901, now named venorphin, which was designed as a chimeric construct of a cobra venom tetrapeptide and [D-Ala8]dynorphin A(1–11)NH2 [1]. The N-terminal region of this new peptide exhibits structure-activity relationships (SAR) distinctly different from that of [D-Ala8]dynorphin A(1–11)NH2 [2]. Herein we explore the SAR of the C-terminal region of venorphin.
Keywords
Opioid Receptor Radioligand Binding Truncation Study Coupling Reagent Kappa Opioid Receptor
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References
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