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The multifunctional host\u2010defence peptides (HDPs) cathelicidins play crucial roles in inflammation. Here, we show that the antimicrobial and immunomodulatory polypeptide human cathelicidin LL\u201037 binds IAPP with nanomolar affinity and effectively suppresses its amyloid self\u2010assembly and related pancreatic \u03b2\u2010cell damage in\u2005vitro. In addition, we identify key LL\u201037 segments that mediate its interaction with IAPP. Our results suggest a possible protective role for LL\u201037 in T2D pathogenesis and offer a molecular basis for the design of LL\u201037\u2010derived peptides that combine antimicrobial, immunomodulatory, and T2D\u2010related anti\u2010amyloid functions as promising candidates for multifunctional drugs.<\/jats:p>","DOI":"10.1002\/anie.202000148","type":"journal-article","created":{"date-parts":[[2020,1,30]],"date-time":"2020-01-30T12:57:24Z","timestamp":1580389044000},"page":"12837-12841","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":53,"title":["The Human Host\u2010Defense Peptide Cathelicidin LL\u201037 is a Nanomolar Inhibitor of Amyloid Self\u2010Assembly of Islet Amyloid Polypeptide (IAPP)"],"prefix":"10.1002","volume":"59","author":[{"given":"Valentina","family":"Armiento","sequence":"first","affiliation":[{"name":"Division of Peptide Biochemistry TUM School of Life Sciences  Emil-Erlenmeyer-Forum 5 85354 Freising 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