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Recent Structure-Activity Studies of the Peptide Hormone Urotensin-II, a Potent Vasoconstrictor

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Abstract:

Human Urotensin-II is a potent vasoconstrictor and binds with high affinity to GPR14 receptor, recently cloned and renamed UT receptor. U-II vasoconstrictive potency is reported to be an order of magnitude greater than that of endothelin-1 (ET-1), which would make it the most potent mammalian vasoconstrictor identified to date.

Urotensin-II is a neuropeptide “somatostatin-like” cyclic peptide, which was originally isolated from fish spinal cords, and which has recently been cloned from human. Human U-II is composed of only 11 amino acids residues, while fish and frog U-II possess 12 and 13 amino acids residues, respectively. The cyclic region of U-II, which is responsible for the biological activity of the peptide, has been fully conserved from fish to human.

This review focuses on recent structure-activity relationships studies performed on Urotensin-II with the aim to provide the required structural elements to design new ligands as agonists and antagonists for UT receptor.

Keywords: ligands; nmr studies; sars studies; urotensin-II

Document Type: Review Article

DOI: https://doi.org/10.2174/0929867043455495

Affiliations: Department of Pharmaceutical and Toxicological Chemistry, University of Naples “Federico II”, Via D. Montesano, 49 “ 80131 ” Naples, ITALY.

Publication date: 2004-04-01

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