Structure-guided, single-point modifications in the phosphinic dipeptide structure yield highly potent and selective inhibitors of neutral aminopeptidases

Journal of Medicinal Chemistry

Volumn 57, Issue 19, 2014, Pages 8140-8151

  Vassiliou, Stamatia ^a   Węglarz Tomczak, Ewelina ^b   Berlicki, L ^b   Pawełczak, Małgorzata ^c   Nocek, Bogusław ^d   Mulligan, Rory ^d   Joachimiak, Andrzej ^d   Mucha, Artur ^b  

^a UNIVERSITY OF ATHENS   (Greece)

^b WROCLAW UNIVERSITY OF TECHNOLOGY   (Poland)

^c UNIVERSITY OF OPOLE   (Poland)

^d ARGONNE NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIPEPTIDE DERIVATIVE; HYDROGEN; MICROSOMAL AMINOPEPTIDASE; PEPTIDE HYDROLASE INHIBITOR; PHOSPHINIC ACID DERIVATIVE; AMINOPEPTIDASE; CYTOSOL AMINOPEPTIDASE; PROTEINASE INHIBITOR;

ARTICLE; BINDING AFFINITY; CRYSTAL STRUCTURE; DRUG INHIBITION; DRUG POTENCY; DRUG SELECTIVITY; ENANTIOMER; ENZYME ACTIVE SITE; HUMAN; HYDROGEN BOND; NEISSERIA MENINGITIDIS; NONHUMAN; STEREOSPECIFICITY; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY; ANTAGONISTS AND INHIBITORS; BINDING SITE; CHEMISTRY; DRUG DESIGN; SYNTHESIS;

AMINOPEPTIDASES; BINDING SITES; DRUG DESIGN; HUMANS; LEUCYL AMINOPEPTIDASE; PROTEASE INHIBITORS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84907900900     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm501071f     Document Type: Article

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