ALPHA-MERCAPTOACYL DIPEPTIDES THAT INHIBIT ANGIOTENSIN-CONVERTING ENZYME AND NEUTRAL ENDOPEPTIDASE-24.11

alpha-Mercaptoacyl dipeptides were prepared and found to inhibit angio tensin converting enzyme (ACE) and neutral endopeptidase 24.11 (NEP). Compounds with a proline as the C-terminal amino acid, and possessing the S-stereochemistry at the thiol bearing carbon were preferred for o ptimal ACE inhibition while, R-stereochemistry was preferred for optim al NEP inhibition. Compounds containing alternative amino acid residue s at the C-terminal position displayed optimal dual ACE/NEP inhibition when the stereochemistry was 'S' at this carbon atom.