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The formation of fibrils via LLPS has been demonstrated for a number of proteins related to neurodegenerative disorders, as well as other amyloidoses. Despite the surge in amyloid\u2010related LLPS studies, the influence of protein condensate formation on the end\u2010point fibril characteristics is still far from fully understood. In this work, we compare alpha\u2010synuclein aggregation under different conditions, which promote or negate its LLPS and examine the differences between the formed aggregates. We show that alpha\u2010synuclein phase separation generates a wide variety of assemblies with distinct secondary structures and morphologies. The LLPS\u2010induced structures also possess higher levels of toxicity to cells, indicating that biomolecular condensate formation may be a critical step in the appearance of disease\u2010related fibril variants.<\/jats:p>","DOI":"10.1111\/febs.17244","type":"journal-article","created":{"date-parts":[[2024,8,8]],"date-time":"2024-08-08T13:14:20Z","timestamp":1723122860000},"page":"4522-4538","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":29,"title":["Liquid\u2013liquid phase separation of alpha\u2010synuclein increases the structural variability of fibrils formed during amyloid aggregation"],"prefix":"10.1111","volume":"291","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8368-6188","authenticated-orcid":false,"given":"Mantas","family":"Ziaunys","sequence":"first","affiliation":[{"name":"Institute of Biotechnology, Life Sciences Center Vilnius University  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