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Although the amyloid\u2010forming proteins have different structures and sequences, all undergo a conformational change to form amyloid aggregates that have a characteristic cross\u2010\u03b2\u2010structure. The mechanistic details of this process are poorly understood, but different strategies for the development of inhibitors of amyloid formation have been proposed. In most cases, chemically diverse compounds bind to an elongated form of the protein in a \u03b2\u2010strand conformation and thereby exert their therapeutic effect. However, this approach could favor the formation of prefibrillar oligomeric species, which are thought to be toxic. Herein, we report an alternative approach in which a helical coiled\u2010coil\u2010based inhibitor peptide has been designed to engage a coiled\u2010coil\u2010based amyloid\u2010forming model peptide in a stable coiled\u2010coil arrangement, thereby preventing rearrangement into a \u03b2\u2010sheet conformation and the subsequent formation of amyloid\u2010like fibrils. Moreover, we show that the helix\u2010forming peptide is able to disassemble mature amyloid\u2010like fibrils.<\/jats:p>","DOI":"10.1002\/chem.201100670","type":"journal-article","created":{"date-parts":[[2011,8,16]],"date-time":"2011-08-16T12:20:29Z","timestamp":1313497229000},"page":"10651-10661","source":"Crossref","is-referenced-by-count":23,"title":["Inhibition of Amyloid Aggregation by Formation of Helical Assemblies"],"prefix":"10.1002","volume":"17","author":[{"given":"Enrico","family":"Brandenburg","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hans","family":"von\u2005Berlepsch","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ulla I. 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