Premium
Urantide Conformation and Interaction with the Urotensin‐ II Receptor
Author(s) -
Brancaccio Diego,
Limatola Antonio,
Campiglia Pietro,
GomezMonterrey Isabel,
Novellino Ettore,
Grieco Paolo,
Carotenuto Alfonso
Publication year - 2014
Publication title -
archiv der pharmazie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 61
eISSN - 1521-4184
pISSN - 0365-6233
DOI - 10.1002/ardp.201300269
Subject(s) - urotensin ii , chemistry , receptor , antagonist , peptide , small molecule , disulfide bond , stereochemistry , ligand (biochemistry) , biochemistry
Urotensin II (U‐II) is a disulfide bridged peptide hormone identified as the ligand of a G protein‐coupled receptor. Human U‐II (H‐Glu‐Thr‐Pro‐Asp‐c[Cys‐Phe‐Trp‐Lys‐Tyr‐Cys]‐Val‐OH) has been described as the most potent vasoconstrictor compound identified to date. We have previously identified the compound termed urantide (H‐Asp‐c[Pen‐Phe‐DTrp‐Orn‐Tyr‐Cys]‐Val‐OH), which is the most potent UT receptor (UTR) antagonist described to date. Urantide may have potential clinical value in the treatment of atherosclerosis. In the present study, we studied the conformational preferences of urantide in DPC micelles and developed a urantide/UTR interaction model. This model can help the design of novel peptides and small molecules as UTR antagonists.