New insight into the binding mode of peptides at urotensin-II receptor by Trp-constrained analogues of P5U and urantide (pages 293–300)
Alfonso Carotenuto, Luigia Auriemma, Francesco Merlino, Antonio Limatola, Pietro Campiglia, Isabel Gomez-Monterrey, Roberta d'Emmanuele di Villa Bianca, Diego Brancaccio, Paolo Santicioli, Stefania Meini, Carlo Alberto Maggi, Ettore Novellino and Paolo Grieco
Article first published online: 25 MAR 2013 | DOI: 10.1002/psc.2498
Human U-II (hU-II) is a disulfide bridged peptide hormone. It is described as the most potent vasoconstrictor compound identified to date. We have recently identified both a superagonist and an antagonist of hU-II termed P5U and urantide, respectively. We have synthesized four analogues of P5U and urantide in which Trp7 was replaced by the highly constrained l-Tpi or d-Tpi residue. This replacement led to active analogues, which allowed improving the knowledge on structure–activity relationships.