{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,16]],"date-time":"2026-05-16T19:19:13Z","timestamp":1778959153861,"version":"3.51.4"},"reference-count":36,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2022,5,25]],"date-time":"2022-05-25T00:00:00Z","timestamp":1653436800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Neurosci."],"abstract":"<jats:p>The intracellular aggregation of \u03b1-synuclein in neurons\/glia is considered to be a key step in the pathogenesis of synucleinopathy [including Parkinson\u2019s disease (PD), dementia with Lewy body (DLB), multiple system atrophy (MSA), etc.]. Increasing evidence indicates that the initial pathological \u03b1-synuclein aggregates can replicate themselves and propagate in a \u201cseeding\u201d manner to multiple areas of the brain and even to peripheral tissue, which makes it the most important biomarker for the diagnosis of synucleinopathies in recent years. The amplification and propagation capabilities of \u03b1-synuclein aggregates are very similar to those of prion-like diseases, which are based on the inherent self-recruitment capabilities of existing misfolded proteins. <jats:italic>In vitro<\/jats:italic>, the rapid recruitment process can be reproduced in a simplified model by adding a small amount of \u03b1-synuclein pre-formed fibrils to the monomer solution as fibril seeds, which may partially reveal the properties of \u03b1-synuclein aggregates. In this study, we explored the elongation rate of \u03b1-synuclein pre-formed fibrils under a quiescent incubation condition (rather than shaking\/agitating). By using the ThT fluorescence assay, we compared and quantified the elongation fluorescence curves to explore the factors that affect fibril elongation. These factors include proteins\u2019 concentration, temperature, NaCl strength, SDS, temperature pretreatment, and so on. Our work further describes the elongation of \u03b1-synuclein fibrils under quiescent incubation conditions. This may have important implications for the <jats:italic>in vitro<\/jats:italic> amplification and preservation of \u03b1-synuclein aggregates to further understand the prion-like transmission mechanism of PD.<\/jats:p>","DOI":"10.3389\/fnins.2022.902077","type":"journal-article","created":{"date-parts":[[2022,5,25]],"date-time":"2022-05-25T13:03:31Z","timestamp":1653483811000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":10,"title":["Quiescent Elongation of \u03b1-Synuclein Pre-form Fibrils Under Different Solution Conditions"],"prefix":"10.3389","volume":"16","author":[{"given":"Hengxu","family":"Mao","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yongyi","family":"Ye","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xiang","family":"Sun","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chen","family":"Qian","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Baoyan","family":"Wang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Linghai","family":"Xie","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shizhong","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1965","published-online":{"date-parts":[[2022,5,25]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"8069","DOI":"10.1073\/pnas.83.21.8069","article-title":"Temperature dependence of the hydrophobic interaction in protein folding.","volume":"83","author":"Baldwin","year":"1986","journal-title":"Proc. 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