{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Schifano F"],"funding":["Ministry of Education, Universities and Research"],"pagination":["791"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10135331"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(4)"],"pubmed_abstract":["α-Synuclein (αS), dopamine (DA), and iron have a crucial role in the etiology of Parkinson's disease. The present study aims to investigate the interplay between these factors by analyzing the DA/iron interaction and how it is affected by the presence of the C-terminal fragment of αS (Ac-αS<sub>119-132</sub>) that represents the iron-binding domain. At high DA:Fe molar ratios, the formation of the [Fe<sup>III</sup>(DA)<sub>2</sub>]<sup>-</sup> complex prevents the interaction with αS peptides, whereas, at lower DA:Fe molar ratios, the peptide is able to compete with one of the two coordinated DA molecules. This interaction is also confirmed by HPLC-MS analysis of the post-translational modifications of the peptide, where oxidized αS is observed through an inner-sphere mechanism. Moreover, the presence of phosphate groups in Ser129 (Ac-αS<sup>p</sup>S<sub>119-132</sub>) and both Ser129 and Tyr125 (Ac-αS<sup>p</sup>Y<sup>p</sup>S<sub>119-132</sub>) increases the affinity for iron(III) and decreases the DA oxidation rate, suggesting that this post-translational modification may assume a crucial role for the αS aggregation process. Finally, αS interaction with cellular membranes is another key aspect for αS physiology. Our data show that the presence of a membrane-like environment induced an enhanced peptide effect over both the DA oxidation and the [Fe<sup>III</sup>(DA)<sub>2</sub>]<sup>-</sup> complex formation and decomposition."],"journal":["Antioxidants (Basel, Switzerland)"],"pubmed_title":["Interaction and Redox Chemistry between Iron, Dopamine, and Alpha-Synuclein C-Terminal Peptides."],"pmcid":["PMC10135331"],"funding_grant_id":["2015T778JW"],"pubmed_authors":["Schifano F","Casella L","Nicolis S","Monzani E","Dell'Acqua S"],"additional_accession":[]},"is_claimable":false,"name":"Interaction and Redox Chemistry between Iron, Dopamine, and Alpha-Synuclein C-Terminal Peptides.","description":"α-Synuclein (αS), dopamine (DA), and iron have a crucial role in the etiology of Parkinson's disease. The present study aims to investigate the interplay between these factors by analyzing the DA/iron interaction and how it is affected by the presence of the C-terminal fragment of αS (Ac-αS<sub>119-132</sub>) that represents the iron-binding domain. At high DA:Fe molar ratios, the formation of the [Fe<sup>III</sup>(DA)<sub>2</sub>]<sup>-</sup> complex prevents the interaction with αS peptides, whereas, at lower DA:Fe molar ratios, the peptide is able to compete with one of the two coordinated DA molecules. This interaction is also confirmed by HPLC-MS analysis of the post-translational modifications of the peptide, where oxidized αS is observed through an inner-sphere mechanism. Moreover, the presence of phosphate groups in Ser129 (Ac-αS<sup>p</sup>S<sub>119-132</sub>) and both Ser129 and Tyr125 (Ac-αS<sup>p</sup>Y<sup>p</sup>S<sub>119-132</sub>) increases the affinity for iron(III) and decreases the DA oxidation rate, suggesting that this post-translational modification may assume a crucial role for the αS aggregation process. Finally, αS interaction with cellular membranes is another key aspect for αS physiology. Our data show that the presence of a membrane-like environment induced an enhanced peptide effect over both the DA oxidation and the [Fe<sup>III</sup>(DA)<sub>2</sub>]<sup>-</sup> complex formation and decomposition.","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Mar","modification":"2025-04-04T11:05:53.638Z","creation":"2025-04-04T11:05:53.638Z"},"accession":"S-EPMC10135331","cross_references":{"pubmed":["37107166"],"doi":["10.3390/antiox12040791"]}}