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Because of the structural similarities between the amyloid species characterizing these diseases, (despite the lack of amino acid homology) it is believed that there might be a common mechanism of toxicity for these conditions. Thus, inhibition of amyloid formation could be a promising disease\u2010modifying therapeutic strategy for them. Aromatic residues have been identified as crucial in formation and stabilization of amyloid structures. This finding was corroborated by high\u2010resolution structural studies, theoretical analysis, and molecular dynamics simulations. Amongst the aromatic entities, tryptophan was found to possess the most amyloidogenic potential. We therefore postulate that targeting aromatic recognition interfaces by tryptophan could be a useful approach for inhibiting the formation of amyloids. Quinones are known as inhibitors of cellular metabolic pathways, to have anti\u2010 cancer, anti\u2010viral and anti\u2010bacterial properties and were shown to inhibit aggregation of several amyloidogenic proteins <jats:italic>in vitro<\/jats:italic>. We have previously described two quinone\u2010tryptophan hybrids which are capable of inhibiting amyloid\u2010beta, the protein associated with AD pathology, both <jats:italic>in vitro<\/jats:italic> and <jats:italic>in vivo<\/jats:italic>. Here we tested their generic properties and their ability to inhibit other amyloidogenic proteins including \u03b1\u2010synuclein, islet amyloid polypeptide, lysozyme, calcitonin, and insulin. Both compounds showed efficient inhibition of all five proteins examined both by ThT fluorescence analysis and by electron microscope imaging. If verified <jats:italic>in vivo<\/jats:italic>, these small molecules could serve as leads for developing generic anti\u2010amyloid drugs. Proteins 2012; \u00a9 2012 Wiley Periodicals, Inc.<\/jats:p>","DOI":"10.1002\/prot.24080","type":"journal-article","created":{"date-parts":[[2012,4,6]],"date-time":"2012-04-06T11:54:54Z","timestamp":1333713294000},"page":"1962-1973","source":"Crossref","is-referenced-by-count":47,"title":["Generic inhibition of amyloidogenic proteins by two naphthoquinone\u2013tryptophan hybrid molecules"],"prefix":"10.1002","volume":"80","author":[{"given":"Roni","family":"Scherzer\u2010Attali","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ronit","family":"Shaltiel\u2010Karyo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yonatan 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