The Replacement of His(4) in Angiotensin IV by Conformationally Constrained Residues Provides Highly Potent and Selective Analogues

Aneta Lukaszuk, Heidi Demaegdt, Debby Feytens, Patrick Vanderheyden, Georges Vauquelin, Dirk Tourwe

Onderzoeksoutput: Articlepeer review

31 Citaten (Scopus)

Samenvatting

The histidine residue in angiotensin IV was replaced by various conformationally constrained amino acids. The substitution of the His4?Pro5 dipeptide sequence by the constrained Trp analogue Aia?Gly, in combination with ?2hVal substitution at the N-terminus, provided a new stable analogue H-(R)-?2hVal-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.
Originele taal-2English
Pagina's (van-tot)5612-5618
Aantal pagina's7
TijdschriftJournal of Medicinal Chemistry
Volume52
Nummer van het tijdschrift18
StatusPublished - 2009

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