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pubmed-article:19757839pubmed:abstractTextThe 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.lld:pubmed
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pubmed-article:19757839pubmed:articleTitleThe replacement of His(4) in angiotensin IV by conformationally constrained residues provides highly potent and selective analogues.lld:pubmed
pubmed-article:19757839pubmed:affiliationDepartment of Organic Chemistry, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium.lld:pubmed
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