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Structural information from a complex of a tetrapeptide renin inhibitor, CP-85,339, with human renin, led to the design of inhibitors with extended P1 groups that span the S1-S3 active site pocket. A m-biphenyl sidechain at P1 and glycine at P3 led to a 160X increase in potency over the analogous phenyl compound. A crystal structure of this compound in complex with recombinant human renin (rHR)...
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