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C\u2010terminally truncated forms of \u03b1\u2010Synuclein are frequently observed in these inclusions in the brains of patients, and their increased aggregation propensity suggests a role in the disease's pathogenesis. This study demonstrates that the small molecule ZPD\u20102 acts as a potent inhibitor of both the spontaneous and seeded amyloid polimerisation of C\u2010terminally truncated \u03b1\u2010Synuclein by interfering with early aggregation intermediates. This dual activity positions this molecule as a promising candidate for therapeutic development in treating synucleinopathies.<\/jats:p>","DOI":"10.1111\/febs.17310","type":"journal-article","created":{"date-parts":[[2024,10,27]],"date-time":"2024-10-27T22:34:23Z","timestamp":1730068463000},"page":"5290-5304","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["The small molecule\n                    <scp>ZPD<\/scp>\n                    \u20102 inhibits the aggregation and seeded polymerisation of C\u2010terminally truncated \u03b1\u2010Synuclein"],"prefix":"10.1111","volume":"291","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2902-823X","authenticated-orcid":false,"given":"Samuel","family":"Pe\u00f1a\u2010D\u00edaz","sequence":"first","affiliation":[{"name":"Institut de Biotecnologia i Biomedicina Universitat Aut\u00f2noma de Barcelona  Bellaterra Spain"},{"name":"Departament de Bioqu\u00edmica i Biologia 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