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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Pepstatin analogues as novel renin inhibitors.

Pepstatin analogues corresponding to the general formula A-X-Y-Sta-Ala-Sta-R were synthesized in solution phase. Various changes in the nature of the A, X, and Y groups were made to improve the inhibitory potency against human plasma renin activity. The results were interpreted by use of the active-site model based on the sequence of human angiotensinogen. The tert-butyloxycarbonyl group and the isovaleryl group were found to be the most effective acyl groups (A). The analogues having a Phe residue in place of Val1 (X) and His or amino acid with an aliphatic side chain such as norleucine or norvaline in the Y position showed the highest inhibition of human plasma renin activity with IC50 values of about 10(-8)M. Esterification or amidification of the carboxyl group of the C-terminal statine did not change the inhibitory potency. The selectivity for rat, dog, pig, and monkey plasma renin of the most interesting compounds was studied.[1]


  1. Pepstatin analogues as novel renin inhibitors. Guégan, R., Diaz, J., Cazaubon, C., Beaumont, M., Carlet, C., Clément, J., Demarne, H., Mellet, M., Richaud, J.P., Segondy, D. J. Med. Chem. (1986) [Pubmed]
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