{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,15]],"date-time":"2026-05-15T20:49:07Z","timestamp":1778878147545,"version":"3.51.4"},"reference-count":38,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2021,5,11]],"date-time":"2021-05-11T00:00:00Z","timestamp":1620691200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100012226","name":"Fundamental Research Funds for the Central Universities","doi-asserted-by":"publisher","award":["201961030"],"award-info":[{"award-number":["201961030"]}],"id":[{"id":"10.13039\/501100012226","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Chemistry &amp; Biodiversity"],"published-print":{"date-parts":[[2021,6]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Amylin (hIAPP) amyloid formation plays an important role in the pathogenesis of type 2 diabetes (T2D), which makes it a promising therapeutic target for T2D. In this study, we established a screening tool for identifying chemicals affecting hIAPP amyloid formation based on a reported genetic tool, which constantly tracks protein aggregates in <jats:italic>Saccharomyces cerevisiae<\/jats:italic>. In order to obtain the hIAPP with better aggregation ability, the gene of hIAPP was tandemly ligated to create 1\u00d7, 2\u00d7, 4\u00d7 or 6\u00d7\u2010hIAPP expressing strains. By measuring the cell density and fluorescence intensity of green fluorescent protein (GFP) regulated by the aggregation status of hIAPP, it was found that four intramolecular ligated hIAPP (4\u00d7hIAPP) could form obvious amyloids with mild toxicity. The validity and reliability of the screening tool were verified by testing six reported hIAPP inhibitors, including curcumin, epigallocatechin gallate and so on. Combined with surface plasmon resonance (SPR) and the screening tool, which could be a screening system for hIAPP inhibitors, we found that crocin specifically binds to hIAPP and acts inhibit amyloid formation of hIAPP. The effect of crocin was further confirmed by Thioflavin T (ThT) fluorescence and transmission electron microscopy (TEM) analysis. Thus, a screening system for hIAPP amyloid inhibitors and a new mechanism of crocin on anti\u2010T2D were obtained as a result of this study.<\/jats:p>","DOI":"10.1002\/cbdv.202100270","type":"journal-article","created":{"date-parts":[[2021,4,23]],"date-time":"2021-04-23T02:20:09Z","timestamp":1619144409000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Identification of Crocin as a New hIAPP Amyloid Inhibitor via a Simple Yet Highly Biospecific Screening System"],"prefix":"10.1002","volume":"18","author":[{"given":"Jingxuan","family":"Lu","sequence":"first","affiliation":[{"name":"Key Laboratory of Marine Drugs Ministry of Education School of Medicine and Pharmacy Ocean University of China  Qingdao 266003 P. R. 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China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wengong","family":"Yu","sequence":"additional","affiliation":[{"name":"Key Laboratory of Marine Drugs Ministry of Education School of Medicine and Pharmacy Ocean University of China  Qingdao 266003 P. R. China"},{"name":"Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology  Qingdao 266003 P. R. China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xinzhi","family":"Lu","sequence":"additional","affiliation":[{"name":"Key Laboratory of Marine Drugs Ministry of Education School of Medicine and Pharmacy Ocean University of China  Qingdao 266003 P. R. 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