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Tertiary-Amine-Based Inhibitors of the Astacin Protease Meprin α.
Tan, Kathrin; Jäger, Christian; Schlenzig, Dagmar; Schilling, Stephan; Buchholz, Mirko; Ramsbeck, Daniel.
Afiliación
  • Tan K; Department of Drug Design and Target Validation MWT, Fraunhofer Institute for Cell Therapy and Immunology IZI, Biocenter, Weinbergweg 22, 06120, Halle (Saale), Germany.
  • Jäger C; Department of Drug Design and Target Validation MWT, Fraunhofer Institute for Cell Therapy and Immunology IZI, Biocenter, Weinbergweg 22, 06120, Halle (Saale), Germany.
  • Schlenzig D; Department of Drug Design and Target Validation MWT, Fraunhofer Institute for Cell Therapy and Immunology IZI, Biocenter, Weinbergweg 22, 06120, Halle (Saale), Germany.
  • Schilling S; Department of Drug Design and Target Validation MWT, Fraunhofer Institute for Cell Therapy and Immunology IZI, Biocenter, Weinbergweg 22, 06120, Halle (Saale), Germany.
  • Buchholz M; Department of Drug Design and Target Validation MWT, Fraunhofer Institute for Cell Therapy and Immunology IZI, Biocenter, Weinbergweg 22, 06120, Halle (Saale), Germany.
  • Ramsbeck D; Department of Drug Design and Target Validation MWT, Fraunhofer Institute for Cell Therapy and Immunology IZI, Biocenter, Weinbergweg 22, 06120, Halle (Saale), Germany.
ChemMedChem ; 13(16): 1619-1624, 2018 08 20.
Article en En | MEDLINE | ID: mdl-29927060
Metalloproteinases of the astacin family are drawing ever increasing attention as potential drug targets. However, knowledge regarding inhibitors thereof is limited in most cases. Crucial for the development of metalloprotease inhibitors is high selectivity, to avoid side effects brought about by inhibition of off-target proteases and interference with physiological pathways. In this study we aimed at the design of novel selective inhibitors for the astacin proteinase meprin α. Based on a recently identified tertiary amine scaffold, a series of compounds was synthesized and evaluated. The compounds exhibit reasonable inhibitory activity with high selectivity over other metalloproteases. The isoenzyme meprinâ€…ß is only slightly inhibited. Hence, the present study revealed a novel class of selective meprin α inhibitors with improved selectivity over known compounds.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Inhibidores de Proteasas / Metaloendopeptidasas / Ácidos Hidroxámicos Límite: Humans Idioma: En Revista: ChemMedChem Asunto de la revista: FARMACOLOGIA / QUIMICA Año: 2018 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Alemania
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Inhibidores de Proteasas / Metaloendopeptidasas / Ácidos Hidroxámicos Límite: Humans Idioma: En Revista: ChemMedChem Asunto de la revista: FARMACOLOGIA / QUIMICA Año: 2018 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Alemania