Your browser doesn't support javascript.
loading
Fragment-Based Discovery and Optimization of Enzyme Inhibitors by Docking of Commercial Chemical Space.
Rudling, Axel; Gustafsson, Robert; Almlöf, Ingrid; Homan, Evert; Scobie, Martin; Warpman Berglund, Ulrika; Helleday, Thomas; Stenmark, Pål; Carlsson, Jens.
Afiliación
  • Rudling A; Department of Biochemistry and Biophysics, Stockholm University , SE-106 91 Stockholm, Sweden.
  • Gustafsson R; Department of Biochemistry and Biophysics, Stockholm University , SE-106 91 Stockholm, Sweden.
  • Almlöf I; Science for Life Laboratory, Department of Medical Biochemistry and Biophysics, Karolinska Institutet , Box 1031, SE-171 21 Solna, Sweden.
  • Homan E; Science for Life Laboratory, Department of Medical Biochemistry and Biophysics, Karolinska Institutet , Box 1031, SE-171 21 Solna, Sweden.
  • Scobie M; Science for Life Laboratory, Department of Medical Biochemistry and Biophysics, Karolinska Institutet , Box 1031, SE-171 21 Solna, Sweden.
  • Warpman Berglund U; Science for Life Laboratory, Department of Medical Biochemistry and Biophysics, Karolinska Institutet , Box 1031, SE-171 21 Solna, Sweden.
  • Helleday T; Science for Life Laboratory, Department of Medical Biochemistry and Biophysics, Karolinska Institutet , Box 1031, SE-171 21 Solna, Sweden.
  • Stenmark P; Department of Biochemistry and Biophysics, Stockholm University , SE-106 91 Stockholm, Sweden.
  • Carlsson J; Science for Life Laboratory, Department of Cell and Molecular Biology, BMC, Uppsala University , Box 596, SE-751 24 Uppsala, Sweden.
J Med Chem ; 60(19): 8160-8169, 2017 10 12.
Article en En | MEDLINE | ID: mdl-28929756
Fragment-based lead discovery has emerged as a leading drug development strategy for novel therapeutic targets. Although fragment-based drug discovery benefits immensely from access to atomic-resolution information, structure-based virtual screening has rarely been used to drive fragment discovery and optimization. Here, molecular docking of 0.3 million fragments to a crystal structure of cancer target MTH1 was performed. Twenty-two predicted fragment ligands, for which analogs could be acquired commercially, were experimentally evaluated. Five fragments inhibited MTH1 with IC50 values ranging from 6 to 79 µM. Structure-based optimization guided by predicted binding modes and analogs from commercial chemical libraries yielded nanomolar inhibitors. Subsequently solved crystal structures confirmed binding modes predicted by docking for three scaffolds. Structure-guided exploration of commercial chemical space using molecular docking gives access to fragment libraries that are several orders of magnitude larger than those screened experimentally and can enable efficient optimization of hits to potent leads.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Inhibidores Enzimáticos / Descubrimiento de Drogas Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: J Med Chem Asunto de la revista: QUIMICA Año: 2017 Tipo del documento: Article País de afiliación: Suecia Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Inhibidores Enzimáticos / Descubrimiento de Drogas Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: J Med Chem Asunto de la revista: QUIMICA Año: 2017 Tipo del documento: Article País de afiliación: Suecia Pais de publicación: Estados Unidos