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C-Terminal Structure-Activity Relationships for the Novel Opioid Peptide JVA-901 (Venorphin)
Book chapter

C-Terminal Structure-Activity Relationships for the Novel Opioid Peptide JVA-901 (Venorphin)

Christy A. Sasiela, Marco A. Bennett, Thomas F. Murray and Jane V. Aldrich
Peptides: The Wave of the Future, pp.689-690
American Peptide Symposia, Springer Netherlands
2001
DOI: https://doi.org/10.1007/978-94-010-0464-0_321

Abstract

Coupling Reagent Kappa Opioid Receptor Opioid Receptor Radioligand Binding Truncation Study
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.

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