Document Report Card

ID: ALA1154281

Journal: J Med Chem

Title: The replacement of His(4) in angiotensin IV by conformationally constrained residues provides highly potent and selective analogues.

Authors: Lukaszuk A, Demaegdt H, Feytens D, Vanderheyden P, Vauquelin G, Tourwé D.

Abstract: The histidine residue in angiotensin IV was replaced by various conformationally constrained amino acids. The substitution of the His(4)-Pro(5) dipeptide sequence by the constrained Trp analogue Aia-Gly, in combination with beta(2)hVal substitution at the N-terminus, provided a new stable analogue H-(R)-beta(2)hVal-Tyr-Ile-Aia-Gly-Phe-OH (AL-40) that is a potent ligand for the Ang IV receptor IRAP and selective versus AP-N and the AT1 receptor.

CiteXplore: 19757839

DOI: 10.1021/jm900651p