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The Amyloid–Congo Red Interface at Atomic Resolution
Author(s) -
Schütz Anne K.,
Soragni Alice,
Hornemann Simone,
Aguzzi Adriano,
Ernst Matthias,
Böckmann Anja,
Meier Beat H.
Publication year - 2011
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201008276
Subject(s) - congo red , amyloid (mycology) , computer science , gold standard (test) , characterization (materials science) , resolution (logic) , amyloid fibril , point mutation , biochemistry , chemistry , computational biology , nanotechnology , mutation , biology , amyloid β , artificial intelligence , materials science , medicine , pathology , adsorption , inorganic chemistry , disease , gene
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.