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Here we show that a single engineered \u03b2\u2010hairpin\u2010binding protein, the \u03b2\u2010wrapin AS10, binds monomers of three different amyloidogenic proteins, that is, amyloid\u2010\u03b2 peptide, \u03b1\u2010synuclein, and islet amyloid polypeptide, with sub\u2010micromolar affinity. AS10 binding inhibits the aggregation and toxicity of all three proteins. The results demonstrate common conformational preferences and related binding sites in a subset of the amyloidogenic proteins. These commonalities enable the generation of multispecific monomer\u2010binding agents.<\/jats:p>","DOI":"10.1002\/cbic.201402552","type":"journal-article","created":{"date-parts":[[2014,12,30]],"date-time":"2014-12-30T16:06:47Z","timestamp":1419955607000},"page":"411-414","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":27,"title":["A \u03b2\u2010Hairpin\u2010Binding Protein for Three Different Disease\u2010Related Amyloidogenic Proteins"],"prefix":"10.1002","volume":"16","author":[{"given":"Hamed","family":"Shaykhalishahi","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ewa A.","family":"Mirecka","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Aziz","family":"Gauhar","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Clara S. 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