{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,20]],"date-time":"2026-06-20T00:00:09Z","timestamp":1781913609980,"version":"3.54.5"},"reference-count":21,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2002,5,29]],"date-time":"2002-05-29T00:00:00Z","timestamp":1022630400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biopolymers"],"published-print":{"date-parts":[[2002,8,5]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Amyloid\u2010like aggregation of \u03b1\u2010synuclein and deposit in Lewy bodies are thought to be the major cause of Parkinson\u2032s disease. Here we describe the secondary structural transformation and aggregation of human \u03b1\u2010synuclein and its C\u2010terminus truncated fragments in trifluoroethanol. Proteins containing the NAC (non\u2010amyloid component) segment undergo a three\u2010state transition: from native random coil to \u03b2\u2010sheet and to \u03b1\u2010helical structure, while the NAC deficient fragment and \u03b3\u2010synuclein undergo a typical two\u2010state coil\u2010to\u2010\u03b1 transition. The \u03b2\u2010sheet form is highly hydrophobic that strongly binds to 1\u2010anilinonaphthalene\u20108\u2010sulfonic acid (ANS) and is prone to self\u2010aggregation. The results suggest that the NAC sequence is essential to \u03b2\u2010sheet formation and the aggregation originates from the \u03b2\u2010sheet intermediate, which may be implicated in the pathogenesis of Parkinson\u2032s disease. \u00a9 2002 Wiley Periodicals, Inc. Biopolymers 64: 221\u2013226, 2002<\/jats:p>","DOI":"10.1002\/bip.10179","type":"journal-article","created":{"date-parts":[[2002,10,6]],"date-time":"2002-10-06T11:25:39Z","timestamp":1033903539000},"page":"221-226","source":"Crossref","is-referenced-by-count":71,"title":["Structural transformation and aggregation of human \u03b1\u2010synuclein in trifluoroethanol: Non\u2010amyloid component sequence is essential and \u03b2\u2010sheet formation is prerequisite to aggregation"],"prefix":"10.1002","volume":"64","author":[{"given":"Hong\u2010Tao","family":"Li","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hai\u2010Ning","family":"Du","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lin","family":"Tang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jun","family":"Hu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hong\u2010Yu","family":"Hu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2002,5,29]]},"reference":[{"key":"e_1_2_6_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0166-2236(97)01213-7"},{"key":"e_1_2_6_3_2","doi-asserted-by":"publisher","DOI":"10.1038\/42166"},{"key":"e_1_2_6_4_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.276.5321.2045"},{"key":"e_1_2_6_5_2","first-page":"4190","volume":"84","author":"Ueda K.","year":"1993","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_2_6_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0959-440X(98)80101-2"},{"key":"e_1_2_6_7_2","doi-asserted-by":"publisher","DOI":"10.1098\/rstb.1994.0041"},{"key":"e_1_2_6_8_2","doi-asserted-by":"publisher","DOI":"10.1002\/1097-0282(2001)62:1<15::AID-BIP30>3.0.CO;2-J"},{"key":"e_1_2_6_9_2","doi-asserted-by":"publisher","DOI":"10.1038\/nm0798-755"},{"key":"e_1_2_6_10_2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/BF03183197","volume":"46","author":"Hu H. 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