biostudies-literatureUnknown16(17)Gemignani JFConselho Nacional de Desenvolvimento Cient??fico e Tecnol??gicoFunda????o Carlos Chagas Filho de Amparo ?? Pesquisa do Estado do Rio de JaneiroEmerging 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 capACS chemical neuroscience3385-3397https://www.ebi.ac.uk/biostudies/studies/S-EPMC12412103biostudies-literatureAn Amyloidogenic Fragment of the Spike Protein from SARS-CoV-2 Virus Stimulates the Aggregation and Toxicity of Parkinson's Disease Protein Alpha-Synuclein.PMC12412103Gemignani JFFollmer CLi MHIzecksohn DEliezer DDabkiewicz DCordeiro YWiecikowski AFNetz PAfalseAn Amyloidogenic Fragment of the Spike Protein from SARS-CoV-2 Virus Stimulates the Aggregation and Toxicity of Parkinson's Disease Protein Alpha-Synuclein.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 cap2025-01-01T00:00:00Z2025 Sep2026-05-29T19:51:52.713Z2026-04-08T05:53:02.141ZS-EPMC124121034084535510.1021/acschemneuro.5c00478