{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,30]],"date-time":"2026-08-30T17:09:00Z","timestamp":1788109740353,"version":"build-2803163510"},"reference-count":71,"publisher":"Wiley","issue":"16","license":[{"start":{"date-parts":[[2022,6,21]],"date-time":"2022-06-21T00:00:00Z","timestamp":1655769600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100004608","name":"Natural Science Foundation of Jiangsu Province","doi-asserted-by":"publisher","award":["BK20200036"],"award-info":[{"award-number":["BK20200036"]}],"id":[{"id":"10.13039\/501100004608","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["chemistry-europe.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["ChemBioChem"],"published-print":{"date-parts":[[2022,8,17]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The aggregation of \u03b1\u2010synuclein (\u03b1\u2010Syn) is a critical pathological hallmark of Parkinson's disease (PD). Prevention of \u03b1\u2010Syn aggregation has become a key strategy for treating PD. Recent studies have suggested that \u03b1\u2010Syn undergoes liquid\u2010liquid phase separation (LLPS) to facilitate nucleation and amyloid formation. Here, we examined the modulation of \u03b1\u2010Syn aggregation by myricetin, a polyhydroxyflavonol compound, under the conditions of LLPS. Unexpectedly, neither the initial morphology nor the phase\u2010separated fraction of \u03b1\u2010Syn was altered by myricetin. However, the dynamics of \u03b1\u2010Syn condensates decreased upon myricetin binding. Further studies showed that myricetin dose\u2010dependently inhibits amyloid aggregation in the condensates by delaying the liquid\u2010to\u2010solid phase transition. In addition, myricetin could disassemble the preformed \u03b1\u2010Syn amyloid aggregates matured from the condensates. Together, our study shows that myricetin inhibits \u03b1\u2010Syn amyloid aggregation in the condensates by retarding the liquid\u2010to\u2010solid phase transition and reveals that \u03b1\u2010Syn phase transition can be targeted to inhibit amyloid aggregation.<\/jats:p>","DOI":"10.1002\/cbic.202200216","type":"journal-article","created":{"date-parts":[[2022,6,3]],"date-time":"2022-06-03T12:29:21Z","timestamp":1654259361000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":52,"title":["Myricetin Inhibits \u03b1\u2010Synuclein Amyloid Aggregation by Delaying the Liquid\u2010to\u2010Solid Phase Transition"],"prefix":"10.1002","volume":"23","author":[{"given":"Bingkuan","family":"Xu","sequence":"first","affiliation":[{"name":"Jiangsu Key Laboratory for Molecular and Medical Biotechnology College of Life Sciences Nanjing Normal University  No.\u20051 Wenyuan Road Nanjing 210046 P.\u2005R. 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