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Interactions of amyloidogenic polypeptides with other proteins are important modulators of self\u2010assembly. Here we present a hot\u2010segment\u2010linking approach to design a series of mimics of the IAPP cross\u2010amyloid interaction surface with A\u03b2 (ISMs) as nanomolar inhibitors of amyloidogenesis and cytotoxicity of A\u03b2, IAPP, or both polypeptides. The nature of the linker determines ISM structure and inhibitory function including both potency and target selectivity. Importantly, ISMs effectively suppress both self\u2010 and cross\u2010seeded IAPP self\u2010assembly. Our results provide a novel class of highly potent peptide leads for targeting protein aggregation in Alzheimer\u2019s disease, type 2 diabetes, or both diseases and a chemical approach to inhibit amyloid self\u2010assembly and pathogenic interactions of other proteins as well.<\/jats:p>","DOI":"10.1002\/anie.201504973","type":"journal-article","created":{"date-parts":[[2015,9,4]],"date-time":"2015-09-04T08:41:52Z","timestamp":1441356112000},"page":"13095-13100","source":"Crossref","is-referenced-by-count":75,"title":["A Hot\u2010Segment\u2010Based Approach for the Design of Cross\u2010Amyloid Interaction Surface Mimics as Inhibitors of Amyloid 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