Key result
This review summarizes the development of peptide and nonpeptide urotensin-II structures to aid in the rational design of new molecules with high affinity for the UT receptor.
This review summarizes the structural development of urotensin-II ligands, providing a foundation for designing novel UT receptor modulators for cardiovascular diseases.
Provides structural basis for UT ligand design; leaves open clinical translation in cardiovascular disease.
Urotensin-II was originally isolated from the goby urophysis in the 1960s as a vasoactive peptide with a prominent role in cardiovascular homeostasis. The identification of human isoform of urotensin-II and its specific UT receptor by Ames et al. in 1999 led to investigating the putative role of the interaction U-II/UT receptor in multiple pathophysiological effects in humans. Since urotensin-II is widely expressed in several peripheral tissues including cardiovascular system, the design and development of novel urotensin-II analogues can improve knowledge about structure-activity relationships (SAR). In particular, since the modulation of the U-II system offers a great potential for therapeutic strategies related to the treatment of several diseases, like cardiovascular diseases, the research of selective and potent ligands at UT receptor is more fascinating. In this paper, we review the developments of peptide and nonpeptide U-II structures so far developed in order to contribute also to a more rational and detectable design and synthesis of new molecules with high affinity at the UT receptor.
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Merlino et al. (2013) conducted a review in Cardiovascular diseases. Urotensin-II Ligands was evaluated. This review summarizes the development of peptide and nonpeptide urotensin-II structures to aid in the rational design of new molecules with high affinity for the UT receptor.
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