{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,20]],"date-time":"2026-08-20T08:23:44Z","timestamp":1787214224659,"version":"build-2736575974"},"reference-count":50,"publisher":"Wiley","issue":"9","license":[{"start":{"date-parts":[[2026,8,5]],"date-time":"2026-08-05T00:00:00Z","timestamp":1785888000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"},{"start":{"date-parts":[[2026,8,5]],"date-time":"2026-08-05T00:00:00Z","timestamp":1785888000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Journal of Peptide Science"],"published-print":{"date-parts":[[2026,9]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    \u03b1\u2010Synuclein (\u03b1Syn) is a major component of pathogenic Lewy bodies and Lewy neurites and is closely associated with Parkinson's disease. Among the various posttranslational modifications of \u03b1Syn, several have been implicated in the degeneration of dopaminergic neurons and are thought to promote Parkinson's disease through enhanced misfolding, aggregation, and accumulation of \u03b1Syn. Two such modifications, phosphorylation at Ser\n                    <jats:sup>129<\/jats:sup>\n                    (S129Phos) and hydroxylation at Tyr\n                    <jats:sup>136<\/jats:sup>\n                    (Y136DOPA), exert distinct effects on \u03b1Syn aggregation: S129Phos has been reported to either inhibit or promote aggregation, whereas Y136DOPA induces the formation of short oligomeric species. To gain insight into the molecular basis underlying the initiation of \u03b1Syn multimerization, we semisynthesized \u03b1Syn carrying either S129Phos or Y136DOPA and prepared recombinant unmodified full\u2010length \u03b1Syn as a control. Vacuum\u2010ultraviolet circular dichroism (VUVCD) spectroscopy revealed that these \u03b1Syn variants in their monomeric states possessed essentially identical secondary structures. These results suggest that the modifications themselves do not induce significant secondary structural changes in monomeric \u03b1Syn.\n                  <\/jats:p>","DOI":"10.1002\/psc.70118","type":"journal-article","created":{"date-parts":[[2026,8,6]],"date-time":"2026-08-06T02:46:23Z","timestamp":1785984383000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["No Significant Secondary Structural Change of \u03b1\u2010Synuclein Monomer by Site\u2010Specific DOPA or Phosphorylation Introduction in Its C\u2010Terminal Region"],"prefix":"10.1002","volume":"32","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7256-3206","authenticated-orcid":false,"given":"Tatsuhito","family":"Matsuo","sequence":"first","affiliation":[{"name":"Department of Medical Radiology, Faculty of Health and Medical Sciences Hiroshima International University  Higashi\u2010Hiroshima Hiroshima 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