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Small-Molecule Inhibitors of Islet Amyloid Polypeptide Fibril Formation

Authors

  • Rajesh Mishra Dr.,

    1. Faculty of Chemistry, Physical Chemistry I—Biophysical Chemistry, Technical University Dortmund, Otto-Hahn-Strasse 6, 44227 Dortmund, Germany, Fax. (+49) 231-755-3901
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  • Bruno Bulic Dr.,

    1. Max-Planck-Institute for Molecular Physiology, Department of Chemical Biology, and Center for Applied Chemical Genomics, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany
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  • Daniel Sellin,

    1. Faculty of Chemistry, Physical Chemistry I—Biophysical Chemistry, Technical University Dortmund, Otto-Hahn-Strasse 6, 44227 Dortmund, Germany, Fax. (+49) 231-755-3901
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  • Suman Jha,

    1. Faculty of Chemistry, Physical Chemistry I—Biophysical Chemistry, Technical University Dortmund, Otto-Hahn-Strasse 6, 44227 Dortmund, Germany, Fax. (+49) 231-755-3901
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  • Herbert Waldmann Prof. Dr.,

    1. Max-Planck-Institute for Molecular Physiology, Department of Chemical Biology, and Center for Applied Chemical Genomics, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany
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  • Roland Winter Prof. Dr.

    1. Faculty of Chemistry, Physical Chemistry I—Biophysical Chemistry, Technical University Dortmund, Otto-Hahn-Strasse 6, 44227 Dortmund, Germany, Fax. (+49) 231-755-3901
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  • Financial support from the DFG, the Fonds der Chemischen Industrie, the country NRW and the EU (Europäischer Fonds für regionale Entwicklung) is gratefully acknowledged.

Abstract

original image

Klein und zackig: Die pathologische Aggregation von Amylin (IAPP), die bei Diabetes mellitus Typ II auftritt, wird durch nanomolare Konzentrationen an niedermolekularen Inhibitoren auf Rhodaninbasis effektiv gehemmt. Diese Wirkung ließ sich rasterkraftmikroskopisch nachweisen (siehe AFM-Bild).

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