Abstract
The endogenous angiotensin II (Ang II) and the synthetic AT2 selective agonist 4-aminoPhe6-Ang II respond very differently to identical cyclizations. Cyclizations of Ang II by thioacetalization, involving the 3 and 5 amino acid residue side chains, provided ligands with almost equipotent binding affinities to Ang II at the AT2 receptor. In contrast, the same cyclization procedures applied on the AT2 selective 4-aminoPhe6-Ang II delivered significantly less potent AT2 receptor ligands, although the AT2/AT1 selectivity was still very high. The fact that different structure–activity relationships are observed after imposing conformational restrictions on Ang II and 4-aminoPhe6-Ang II, respectively, suggests that the peptides, despite large similarities might adopt quite different backbone conformations when binding to the AT2 receptor.
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