Tracing binding modes in hit-to-lead optimization: Chameleon-like poses of aspartic protease inhibitors

Angewandte Chemie - International Edition

Volumn 54, Issue 9, 2015, Pages 2849-2853

  Kuhnert, Maren ^a   Köster, Helene ^a   Bartholomäus, Ruben ^a   Park, Ah Young ^a   Shahim, Amir ^a   Heine, Andreas ^a   Steuber, Holger ^a,b   Klebe, Gerhard ^a   Diederich, Wibke E ^a  

^a PHILIPPS UNIVERSITY MARBURG   (Germany)

^b BAYER PHARMA AG   (Germany)

Author keywords

Drug design; Enzyme inhibitors; Ligand enzyme binding; Structure determination; Thermal shift assay (tsa)

Indexed keywords

BINDING ENERGY; CHEMICAL MODIFICATION; DECISION MAKING; ENZYMES; OUTSOURCING; SCAFFOLDS;

DRUG DESIGN; ENZYME BINDING; ENZYME INHIBITORS; STRUCTURE DETERMINATION; THERMAL SHIFT;

STRUCTURAL OPTIMIZATION;

ASPARTIC PROTEINASE; ENDOTHIAPEPSIN; PROTEINASE INHIBITOR; THIOPHENE DERIVATIVE;

ANTAGONISTS AND INHIBITORS; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; DOSE RESPONSE; DRUG EFFECTS; METABOLISM; STRUCTURE ACTIVITY RELATION; SYNTHESIS;

ASPARTIC ACID ENDOPEPTIDASES; BINDING SITES; DOSE-RESPONSE RELATIONSHIP, DRUG; MODELS, MOLECULAR; MOLECULAR STRUCTURE; PROTEASE INHIBITORS; STRUCTURE-ACTIVITY RELATIONSHIP; THIOPHENES;

EID: 84923068707     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201411206     Document Type: Article

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