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Abstract
Conformationally restricted cyclic analogues of angiotensin II (ANG II), Asp1-Arg2-Val3-Tyr4-Val5-His6-Pro7-Phe8, with a link between positions 3 and 5 have considerable biological activity. It is proposed that the spatial arrangement of the pharmacophore groups of Tyr4, His6 and Phe8 side chains and the C-terminal carboxyl group in ANG II and active analogues is similar. Conformational analysis of ANG II and two cyclic analogues c[Sar1, Lys3,Glu5]ANG II and c[Sar1,Hcy3,Mpt5]ANG II was performed, and a geometrical comparison of the low-energy conformations of these compounds allowed one to propose a model of receptor-bound conformation in terms of the spatial arrangement of the pharmacophore groups. This model is characterised by the close spatial location of the His6-Phe8 side chains and the Tyr4 C-terminal carboxyl group and is stabilised by the electrostatic interaction of Arg2 and the C-terminal carboxyl group.
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