Abstract
A conformational search using high-temperature molecular dynamics on angiotensin II(AII) and on two cyclic S-S bridged analogs, namely [Hcy3,5]AII and [Cys3,5]AII, in conjunction with a cluster analysis based on the similarities of the three-dimensional patterns of the binding and activation elements, had led to putative AII receptor-bound conformations. These conformations are characterized by a compact folded shape of the peptide backbone, and by particular relative positions of the four pharmacophore groups, namely the aromatic moieties of the Tyr4, His6 and Phe8 residues, and the C-terminal carboxyl group. This compact folded shape, arising from attractive electrostatic interactions between the desolvated N- and C-terminal groups, is similar to the crystallographically determined conformation of AII bound to the antibody Fab receptor.
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