{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["16(17)"],"submitter":["Gemignani JF"],"funding":["Conselho Nacional de Desenvolvimento Cient??fico e Tecnol??gico","Funda????o Carlos Chagas Filho de Amparo ?? Pesquisa do Estado do Rio de Janeiro"],"pubmed_abstract":["Emerging evidence suggests that the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection may have long-term deleterious effects on the central nervous system and even contribute to post-COVID neurological syndromes. Interestingly, inflammation-induced proteolytic processing of the Spike protein of SARS-CoV-2 leads to the generation of peptides capable of aggregating into amyloid fibrils <i>in vitro</i>. Herein, we investigate the <i>in vitro</i> effect of a fibrillogenic fragment of the Spike protein [Spike 194-203 (S194)] on the aggregation and toxicity of the Parkinson's disease (PD) protein α-synuclein (αSyn). Our results indicate that S194 fibrils stimulate in a concentration-dependent manner the fibrillation of αSyn monomer, resulting in aggregates with increased cap"],"journal":["ACS chemical neuroscience"],"pagination":["3385-3397"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12412103"],"repository":["biostudies-literature"],"pubmed_title":["An Amyloidogenic Fragment of the Spike Protein from SARS-CoV-2 Virus Stimulates the Aggregation and Toxicity of Parkinson's Disease Protein Alpha-Synuclein."],"pmcid":["PMC12412103"],"pubmed_authors":["Gemignani JF","Follmer C","Li MH","Izecksohn D","Eliezer D","Dabkiewicz D","Cordeiro Y","Wiecikowski AF","Netz PA"],"additional_accession":[]},"is_claimable":false,"name":"An Amyloidogenic Fragment of the Spike Protein from SARS-CoV-2 Virus Stimulates the Aggregation and Toxicity of Parkinson's Disease Protein Alpha-Synuclein.","description":"Emerging evidence suggests that the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection may have long-term deleterious effects on the central nervous system and even contribute to post-COVID neurological syndromes. Interestingly, inflammation-induced proteolytic processing of the Spike protein of SARS-CoV-2 leads to the generation of peptides capable of aggregating into amyloid fibrils <i>in vitro</i>. Herein, we investigate the <i>in vitro</i> effect of a fibrillogenic fragment of the Spike protein [Spike 194-203 (S194)] on the aggregation and toxicity of the Parkinson's disease (PD) protein α-synuclein (αSyn). Our results indicate that S194 fibrils stimulate in a concentration-dependent manner the fibrillation of αSyn monomer, resulting in aggregates with increased cap","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Sep","modification":"2026-05-29T19:51:52.713Z","creation":"2026-04-08T05:53:02.141Z"},"accession":"S-EPMC12412103","cross_references":{"pubmed":["40845355"],"doi":["10.1021/acschemneuro.5c00478"]}}