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Angiotensin II: STUDIES ON THE BIOLOGICALLY ACTIVE CONFORMATION

The conformation at the receptor of angiotensin II has been investigated by chemical modification to restrict the rotational freedom of the peptide backbone. Calculations on N-methyl amino acids have shown a reduction in flexibility of a factor of 2 at the backbone as well as a restriction of the preceding residue to positive values of psi. In addition, α-methyl amino acids restrict the backbone to either right- or left-handed alpha-helical angles at that residue. Consideration of these effects and the biological activity of several angiotensin II analogues place certain constraints on &phis;2,Ψ3,&phis;3,&phis;4,Ψ5,&phis;5, &phis;6and Ψ7 in the biologically active state