<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Bonaccorsi di Patti MC</submitter><funding>Sapienza University of Rome (Progetti di Ricerca)</funding><pagination>1231</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12467708</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>15(9)</volume><pubmed_abstract>This study explores the structural transitions and aggregation behaviour of recombinant β- and γ-synucleins from five vertebrate species-&lt;i>Cyprinus carpio&lt;/i>, &lt;i>Danio rerio&lt;/i>, &lt;i>Xenopus laevis&lt;/i>, &lt;i>Anolis carolinensis,&lt;/i> and &lt;i>Homo sapiens&lt;/i>-using thioflavin T fluorescence and circular dichroism spectroscopy, with and without copper ions. Although synucleins are well-conserved proteins among vertebrates, species-specific differences in amino acid composition and predicted secondary structures were observed, particularly within β-strand-forming regions. During a six-day incubation, human β-synuclein exhibited a time-dependent increase in β-sheet-rich structures, while non-mammalian β-synucleins showed limited variation. In contrast, γ-synucleins from all species displayed grea</pubmed_abstract><journal>Biomolecules</journal><pubmed_title>Comparative Analysis of Aggregation of β- and γ-Synucleins in Vertebrates.</pubmed_title><pmcid>PMC12467708</pmcid><funding_grant_id>RM1201729CB8436F</funding_grant_id><pubmed_authors>Toni M</pubmed_authors><pubmed_authors>Meoni M</pubmed_authors><pubmed_authors>Bonaccorsi di Patti MC</pubmed_authors></additional><is_claimable>false</is_claimable><name>Comparative Analysis of Aggregation of β- and γ-Synucleins in Vertebrates.</name><description>This study explores the structural transitions and aggregation behaviour of recombinant β- and γ-synucleins from five vertebrate species-&lt;i>Cyprinus carpio&lt;/i>, &lt;i>Danio rerio&lt;/i>, &lt;i>Xenopus laevis&lt;/i>, &lt;i>Anolis carolinensis,&lt;/i> and &lt;i>Homo sapiens&lt;/i>-using thioflavin T fluorescence and circular dichroism spectroscopy, with and without copper ions. Although synucleins are well-conserved proteins among vertebrates, species-specific differences in amino acid composition and predicted secondary structures were observed, particularly within β-strand-forming regions. During a six-day incubation, human β-synuclein exhibited a time-dependent increase in β-sheet-rich structures, while non-mammalian β-synucleins showed limited variation. In contrast, γ-synucleins from all species displayed grea</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Aug</publication><modification>2026-05-02T03:20:38.815Z</modification><creation>2026-05-02T03:12:01.365Z</creation></dates><accession>S-EPMC12467708</accession><cross_references><pubmed>41008538</pubmed><doi>10.3390/biom15091231</doi></cross_references></HashMap>