期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 54, 期 7, 页码 2062-2067出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201408744
关键词
amyloid inhibitors; amyloid self-assembly; complementation assays; fluorescence; self-assembly
资金
- Israel Science Foundation (ISF) [449/11]
Amyloid deposits are pathological hallmark of a large group of human degenerative disorders of unrelated etiologies. While accumulating evidence suggests that early oligomers may account for tissue degeneration, most detection tools do not allow the monitoring of early association events. Here we exploit bimolecular fluorescence complementation analysis to detect and quantify the dimerization of three major amyloidogenic polypeptides; islet amyloid polypeptide, beta-amyloid and alpha-synuclein. The constructed systems provided direct visualization of protein-protein interactions in which only assembled dimers display strong fluorescent signal. Potential inhibitors that interfere with the initial intermolecular interactions of islet amyloid polypeptide were further identified using this system. Moreover, the identified compounds were able to inhibit the aggregation and cytotoxicity of islet amyloid polypeptide, demonstrating the importance of targeting amyloid dimer formation for future drug development.
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