Format

Send to

Choose Destination

Links from PubChem BioAssay

See comment in PubMed Commons below
J Med Chem. 2009 Sep 24;52(18):5612-8. doi: 10.1021/jm900651p.

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

Author information

1
Department of Organic Chemistry, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium.

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.

PMID:
19757839
DOI:
10.1021/jm900651p
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for American Chemical Society
    Loading ...
    Support Center