Design and Synthesis of Metabolically Stable tRNA Synthetase Inhibitors Derived from Cladosporin.


Journal

Chembiochem : a European journal of chemical biology
ISSN: 1439-7633
Titre abrégé: Chembiochem
Pays: Germany
ID NLM: 100937360

Informations de publication

Date de publication:
01 03 2019
Historique:
received: 01 10 2018
pubmed: 22 11 2018
medline: 31 12 2019
entrez: 22 11 2018
Statut: ppublish

Résumé

Selective and specific inhibitors of Plasmodium falciparum lysyl-tRNA synthetase represent promising therapeutic antimalarial avenues. Cladosporin was identified as a potent P. falciparum lysyl-tRNA synthetase inhibitor, with an activity against parasite lysyl-tRNA synthetase >100-fold more potent than that of the activity registered against the human enzyme. Despite its compelling activity, cladosporin exhibits poor oral bioavailability; a critical requirement for antimalarial drugs. Thus, the quest to develop metabolically stable cladosporin-derived analogues, while retaining similar selectivity and potency to that of the natural compound, has begun. Chemogenomic profiling of a designed library allowed an entirely innovative structure-activity relationship study to be initiated; this shed light on structural evidence of a privileged scaffold with a unique activity against tRNA synthetases.

Identifiants

pubmed: 30462880
doi: 10.1002/cbic.201800587
doi:

Substances chimiques

Antimalarials 0
Enzyme Inhibitors 0
Isocoumarins 0
cladosporin 81PR0D5FI4
Lysine-tRNA Ligase EC 6.1.1.6

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

644-649

Informations de copyright

© 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

Auteurs

Marion Rusch (M)

NIBR-Novartis Institute for Biomedical Research, Fabrikstrasse 22-1.051.17, 4054, Basel, Switzerland.

Arnaud Thevenon (A)

NIBR-Novartis Institute for Biomedical Research, Fabrikstrasse 22-1.051.17, 4054, Basel, Switzerland.
Department of Chemistry, Imperial College, London, SW7 2AZ, UK.

Dominic Hoepfner (D)

NIBR-Novartis Institute for Biomedical Research, Fabrikstrasse 22-1.051.17, 4054, Basel, Switzerland.

Thomas Aust (T)

NIBR-Novartis Institute for Biomedical Research, Fabrikstrasse 22-1.051.17, 4054, Basel, Switzerland.

Christian Studer (C)

NIBR-Novartis Institute for Biomedical Research, Fabrikstrasse 22-1.051.17, 4054, Basel, Switzerland.

Maude Patoor (M)

NIBR-Novartis Institute for Biomedical Research, Fabrikstrasse 22-1.051.17, 4054, Basel, Switzerland.

Patrick Rollin (P)

Institut de Chimie Organique et Analytique (ICOA), UMR7311, Université d'Orléans, 45100, Orléans, France.

Madeleine Livendahl (M)

NIBR-Novartis Institute for Biomedical Research, Fabrikstrasse 22-1.051.17, 4054, Basel, Switzerland.

Beatrice Ranieri (B)

NIBR-Novartis Institute for Biomedical Research, Fabrikstrasse 22-1.051.17, 4054, Basel, Switzerland.

Esther Schmitt (E)

NIBR-Novartis Institute for Biomedical Research, Fabrikstrasse 22-1.051.17, 4054, Basel, Switzerland.

Carsten Spanka (C)

NIBR-Novartis Institute for Biomedical Research, Fabrikstrasse 22-1.051.17, 4054, Basel, Switzerland.

Karl Gademann (K)

University of Zürich, Department of Chemistry, Winterthurerstrasse 190, 8057, Zürich, Switzerland.

Laure C Bouchez (LC)

NIBR-Novartis Institute for Biomedical Research, Fabrikstrasse 22-1.051.17, 4054, Basel, Switzerland.

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Classifications MeSH