The Amyloid-Congo Red Interface at Atomic Resolution

被引:120
|
作者
Schuetz, Anne K. [2 ]
Soragni, Alice [2 ]
Hornemann, Simone [3 ]
Aguzzi, Adriano [3 ]
Ernst, Matthias [2 ]
Boeckmann, Anja [1 ]
Meier, Beat H. [2 ]
机构
[1] Univ Lyon 1, CNRS, Inst Biol & Chim Prot, UMR 5086, F-69367 Lyon, France
[2] Swiss Fed Inst Technol, CH-8093 Zurich, Switzerland
[3] Univ Spital Zurich, Inst Neuropathol, CH-8091 Zurich, Switzerland
基金
瑞士国家科学基金会;
关键词
amyloids; Congo red; prions; proteins; structure elucidation; ANGLE-SPINNING NMR; PROTEIN AGGREGATION; FIBRILS; BINDING; IDENTIFICATION; MECHANISM;
D O I
10.1002/anie.201008276
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
引用
收藏
页码:5956 / 5960
页数:5
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