{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T13:06:30Z","timestamp":1792069590437,"version":"4.4.0"},"reference-count":80,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2023,2,9]],"date-time":"2023-02-09T00:00:00Z","timestamp":1675900800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R35GM142869"],"award-info":[{"award-number":["R35GM142869"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2023,6]]},"abstract":"<jats:p>\n                    Abrupt aggregation of amyloid \u03b2\n                    <jats:sub>1\u201042<\/jats:sub>\n                    (A\u03b2) peptide is a hallmark of Alzheimer's disease (AD), a severe pathology that affects more than 44\u00a0million people worldwide. A growing body of evidence suggests that lipids can uniquely alter rates of A\u03b2\n                    <jats:sub>1\u201042<\/jats:sub>\n                    aggregation. However, it remains unclear whether lipids only alter rates of protein aggregation or also uniquely modify the secondary structure and toxicity of A\u03b2\n                    <jats:sub>1\u201042<\/jats:sub>\n                    oligomers and fibrils. In this study, we investigated the effect of phosphatidylcholine (PC), cardiolipin (CL), and cholesterol (Chol) on A\u03b2\n                    <jats:sub>1\u201042<\/jats:sub>\n                    aggregation. We found that PC, CL and Chol strongly accelerated the rate of fibril formation compared to the rate of A\u03b2\n                    <jats:sub>1\u201042<\/jats:sub>\n                    aggregation in the lipid\u2010free environment. Furthermore, anionic CL enabled the strongest acceleration of A\u03b2\n                    <jats:sub>1\u201042<\/jats:sub>\n                    aggregation compared to zwitterionic PC and uncharged Chol. We also found that PC, CL and Chol uniquely altered the secondary structure of early\u2010, middle\u2010 and late\u2010stage A\u03b2\n                    <jats:sub>1\u201042<\/jats:sub>\n                    aggregates. Specifically, CL and Chol drastically increased the amount of parallel \u03b2\u2010sheet in A\u03b2\n                    <jats:sub>1\u201042<\/jats:sub>\n                    oligomers and fibrils grown in the presence of these lipids. This caused a significant increase in the toxicity of A\u03b2\u00a0:\u00a0CL and A\u03b2\u00a0:\u00a0Chol compared to the toxicity of A\u03b2\u00a0:\u00a0PC and A\u03b2\n                    <jats:sub>1\u201042<\/jats:sub>\n                    aggregates formed in the lipid\u2010free environment. These results demonstrate that toxicity of A\u03b2 aggregates correlates with the amount of their \u03b2\u2010sheet content, which, in turn, is determined by the chemical structure of lipids present at the stage of A\u03b2\n                    <jats:sub>1\u201042<\/jats:sub>\n                    aggregation.\n                  <\/jats:p>","DOI":"10.1111\/febs.16738","type":"journal-article","created":{"date-parts":[[2023,1,27]],"date-time":"2023-01-27T09:04:00Z","timestamp":1674810240000},"page":"3203-3220","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":66,"title":["Lipids uniquely alter the secondary structure and toxicity of amyloid beta 1\u201342 aggregates"],"prefix":"10.1111","volume":"290","author":[{"given":"Kiryl","family":"Zhaliazka","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Biophysics Texas A&amp;M University  College Station Texas 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