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β-Homo-amino Acid Scan of Angiotensin IV

Authors :
Dirk Tourwé
Erzsebet Szemenyei
Dagmara Tymecka
Aleksandra Misicka
Georges Vauquelin
Philippe Karoyan
Aneta Lukaszuk
Heidi Demaegdt
Patrick Vanderheyden
Géza Tóth
Faculty of Sciences and Bioengineering Sciences
Chemistry
Department of Bio-engineering Sciences
Experimental Pharmacology
Molecular and Biochemical Pharmacology
Organic Chemistry
département de chimie organique
Université libre de Bruxelles (ULB)
Department of Molecular and Biochemical Pharmacology
Vrije Universiteit Brussel (VUB)
Hungarian Academy of Sciences (MTA)
Warsaw University.
University of Warsaw (UW)
Systems Research Institute [Warsaw] (IBS PAN)
Polska Akademia Nauk = Polish Academy of Sciences (PAN)
Université Pierre et Marie Curie - Paris 6 (UPMC)
Pleinlaan 2
Source :
Journal of Medicinal Chemistry, Journal of Medicinal Chemistry, American Chemical Society, 2008, 51 ((7)), pp.2291-6. ⟨10.1021/jm701490g⟩, Journal of Medicinal Chemistry, 2008, 51 ((7)), pp.2291-6. ⟨10.1021/jm701490g⟩
Publication Year :
2008
Publisher :
American Chemical Society (ACS), 2008.

Abstract

International audience; Angiotensin IV, a metabolite of angiotensin II, inhibits the enzyme insulin regulated aminopeptidase or IRAP and also, although with lower potency, aminopeptidase-N (AP-N). When both beta (2)-homo amino acid- and beta (3)-homo amino acid substitutions were used, allowed the identification of H-( R)beta (2)hVal-Tyr-Ile-His-Pro-beta (3)hPhe-OH as a potent and stable Ang IV analog with high selectivity for IRAP versus AP-N and the AT1 receptor.

Details

ISSN :
15204804 and 00222623
Volume :
51
Database :
OpenAIRE
Journal :
Journal of Medicinal Chemistry
Accession number :
edsair.doi.dedup.....8c9c11c2cc7ebd3a17c01cfe5de6e89c