Abstract

We prepared a new series of renin inhibitors based on dipeptide glycols, replacing the P 4−P 3 subsites with an O-(N-morpholinocarbonyl)-3-L-phenyllactic acid residue. This modification proved bioisosteric with Boc-L-phenylalanine, giving rise to highly potent human renin inhibitors (1–5 nM), e.g., SC-46944 (IC 50 = 5 nM). Moreover, this change produced compounds that are orally efficacious in reducing plasma renin activity in salt-depleted marmosets.

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