Phosphorus-containing inhibitors of angiotensin-converting enzyme.

Abstract
Several phosphonamides, phosphoramides and phosphates having the general structure R-Y-P(O)(OH)-X-CH(CH3)-CO-Pro were synthesized and tested for inhibition of angiotensin-converting enzyme (dipeptidyl carboxypeptidase; peptidyldipeptide hydrolase). Inhibition depended on the nature of R, Y, and X such that the maximal effect was observed when X = NH, Y = CH2, and R = .vphi.CH2 (50% inhibition at 7 nM). Substitution of CH2 or O at X and O at Y produced significantly less potent inhibitions. Groups shorter or longer than R = .vphi.CH2 led to less active inhibitors, presumably due to nonoptimal interaction of the side chain with the S1 subsite.

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