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The Amyloid–Congo Red Interface at Atomic Resolution

Authors


  • This work was supported by the ETH Zurich, the Swiss National Science Foundation (Grant 200020_124611), the CNRS, and the Agence Nationale de la Recherche (ANR-07-PCVI-0013-03, ANR-06-BLAN-0266, ANR-PCV08 321323, and ANR08-PCVI-0022-02). We also acknowledge support from the European Commission under the Seventh Framework Programme (FP7), contract Bio-NMR 261863.

Abstract

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The analytical “gold standard” for amyloid characterization and diagnostics, Congo red, was studied in complex with an amyloid (see picture). Based on details of the binding mode, a point mutation of the amyloid was prepared which has the same three-dimensional structure as the wild-type protein but is not congophilic. This surprising specificity may aid in the design of selective anti-amyloidogenic drugs.

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