{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T09:43:22Z","timestamp":1790934202041,"version":"4.1.0"},"reference-count":50,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2008,12,31]],"date-time":"2008-12-31T00:00:00Z","timestamp":1230681600000},"content-version":"vor","delay-in-days":3287,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2000,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>\u03b1\u2010Synuclein, a major constituent of Lewy bodies (LBs) in Parkinson's disease (PD), has been implicated to play a critical role in synaptic events, such as neuronal plasticity during development, learning, and degeneration under pathological conditions, although the physiological function of \u03b1\u2010synuclein has not yet been established. We here present biochemical evidence that recombinant \u03b1\u2010synuclein has a chaperone\u2010like function against thermal and chemical stress in vitro. In our experiments, \u03b1\u2010synuclein protected glutathione S\u2010transferase (GST) and aldolase from heat\u2010induced precipitation, and \u03b1\u2010lactalbumin and bovine serum albumin from dithiothreitol (DTT)\u2010induced precipitation like other molecular chaperones. Moreover, preheating of \u03b1\u2010synuclein, which is believed to reorganize the molecular surface of \u03b1\u2010synuclein, increased the chaperone\u2010like activity. Interestingly, in organic solvents, which promotes the formation of secondary structure, \u03b1\u2010synuclein aggregated more easily than in its native condition, which eventually might abrogate the chaperone\u2010like function of the protein. In addition, \u03b1\u2010synuclien was also rapidly and significantly precipitated by heat in the presence of Zn<jats:sup>2+<\/jats:sup>in vitro, whereas it was not affected by the presence of Ca<jats:sup>2+<\/jats:sup>or Mg<jats:sup>2+<\/jats:sup>. Circular dichroism spectra confirmed that \u03b1\u2010synuclein underwent conformational change in the presence of Zn<jats:sup>2+<\/jats:sup>. Taken together, our data suggest that \u03b1\u2010synuclein could act as a molecular chaperone, and that the conformational change of the \u03b1\u2010synuclein could explain the aggregation kinetics of \u03b1\u2010synuclein, which may be related to the abolishment of the chaperonic\u2010like activity.<\/jats:p>","DOI":"10.1110\/ps.9.12.2489","type":"journal-article","created":{"date-parts":[[2009,2,17]],"date-time":"2009-02-17T22:40:06Z","timestamp":1234910406000},"page":"2489-2496","source":"Crossref","is-referenced-by-count":108,"title":["Structural changes in \u03b1\u2010synuclein affect its chaperone\u2010like activity in vitro"],"prefix":"10.1002","volume":"9","author":[{"given":"Thomas D.","family":"Kim","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Seung 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