Document Report Card

ID: ALA1129797

Journal: J Med Chem

Title: Dual metalloprotease inhibitors. 6. Incorporation of bicyclic and substituted monocyclic azepinones as dipeptide surrogates in angiotensin-converting enzyme/neutral endopeptidase inhibitors.

Authors: Robl JA, Cimarusti MP, Simpkins LM, Brown B, Ryono DE, Bird JE, Asaad MM, Schaeffer TR, Trippodo NC.

Abstract: A series of substituted monocyclic and bicyclic azepinones were incorporated as dipeptide surrogates in mercaptoacetyl dipeptides with the desire to generate a single compound which would potently inhibit both angiotensin-converting enzyme (ACE) and neutral endopeptidase (NEP). Many of these compounds displayed excellent potency against both enzymes. Two of the most potent compounds, monocyclic azepinone 2n and bicyclic azepinone 3q, demonstrated a high level of activity versus ACE and NEP both in vitro and in vivo.

CiteXplore: 8558518

DOI: 10.1021/jm950677a