Optimal recognition of neutral endopeptidase and angiotensin-converting enzyme active sites by mercaptoacyldipeptides as a means to design potent dual inhibitors

Journal of Medicinal Chemistry

Volumn 39, Issue 6, 1996, Pages 1210-1219

  Coric, Pascale ^a   Turcaud, Serge ^a   Meudal, Hervé ^a   Roques, Bernard Pierre ^a   Fournie Zaluski, Marie Claude ^a  

^a Laboratoire de Pharmacochimie   (France)

Author keywords

[No Author keywords available]

Indexed keywords

DIPEPTIDE DERIVATIVE; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; MEMBRANE METALLOENDOPEPTIDASE; N (2 MERCAPTO 3 METHYLBUTANOYL)ISOLEUCYLTYROSINE; N (2 MERCAPTO 3 PHENYLPROPANOYL)ALANYLPROLINE; UNCLASSIFIED DRUG;

BLOOD PRESSURE REGULATION; CONGESTIVE HEART FAILURE; DRUG POTENCY; DRUG SYNTHESIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INHIBITION; HYPERTENSION; MOLECULAR MODEL; MOLECULAR RECOGNITION; NONHUMAN; RENIN ANGIOTENSIN ALDOSTERONE SYSTEM; REVIEW; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ANGIOTENSIN-CONVERTING ENZYME INHIBITORS; ANIMALS; BINDING SITES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NEPRILYSIN; PROTEASE INHIBITORS; RABBITS; RATS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0029970468     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm950590p     Document Type: Review

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