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Using two different experimental techniques, we found that H<jats:sub>2<\/jats:sub>O<jats:sub>2<\/jats:sub> was generated during the aggregation of human amylin into amyloid fibrils. This process was greatly stimulated by Cu(II) ions, and human amylin was retained on a copper affinity column. In contrast, rodent amylin, which is not toxic, failed to generate any H<jats:sub>2<\/jats:sub>O<jats:sub>2<\/jats:sub> and did not interact with copper. We conclude that the formation of H<jats:sub>2<\/jats:sub>O<jats:sub>2<\/jats:sub> from amylin could contribute to the progressive degeneration of islet cells in T2Dm.<\/jats:p>","DOI":"10.1016\/j.febslet.2007.06.061","type":"journal-article","created":{"date-parts":[[2007,7,3]],"date-time":"2007-07-03T11:21:07Z","timestamp":1183461667000},"page":"3489-3493","source":"Crossref","is-referenced-by-count":87,"title":["Copper\u2010mediated formation of hydrogen peroxide from the amylin peptide: A novel mechanism for degeneration of islet cells in type\u20102 diabetes mellitus?"],"prefix":"10.1002","volume":"581","author":[{"given":"Atef","family":"Masad","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lee","family":"Hayes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brian 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