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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, \u03b2\u2010amyloid and \u03b1\u2010synuclein. The constructed systems provided direct visualization of protein\u2010protein 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.<\/jats:p>","DOI":"10.1002\/anie.201408744","type":"journal-article","created":{"date-parts":[[2014,12,22]],"date-time":"2014-12-22T20:41:16Z","timestamp":1419280876000},"page":"2062-2067","source":"Crossref","is-referenced-by-count":21,"title":["Monitoring and Targeting the Initial Dimerization Stage of Amyloid 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