{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Elbatrawy AA"],"funding":["Boston University","Edward Lowe Foundation","NIA NIH HHS","Michigan State University","NINDS NIH HHS","Robert J. Kleberg, Jr. and Helen C. Kleberg Foundation","NIH","Alzheimer's Association","Lowe Foundation"],"pagination":["117990"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11645236"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["116"],"pubmed_abstract":["Tau and α-synuclein (α-syn) are prone-to-aggregate proteins that can be responsible for pathological lesions found in the brains of Alzheimer's disease (AD), Lewy body dementia (LBD), and Parkinson's disease (PD) patients. The early-stage oligomers and protofibrils of tau are believed to be strongly linked to human cognitive impairment while the toxic α-syn oligomers are associated with behavioral motor deficits. Therefore, concurrent targeting of both proteinaceous aggregates and oligomers are very challenging. Herein, rhodanine-based compounds were designed and synthesized to target the fibrils and oligomers of tau and α-syn proteins. In particular, the indole-containing rhodanines 5l and 5r displayed significantly high anti-aggregation activity towards α-syn fibrils by reducing of the t"],"journal":["Bioorganic & medicinal chemistry"],"pubmed_title":["Exploring the rhodanine universe: Design and synthesis of fluorescent rhodanine-based derivatives as anti-fibrillar and anti-oligomer agents against α-synuclein and 2N4R tau."],"pmcid":["PMC11645236"],"funding_grant_id":["R21 NS121826","K08 AG071985","NS121826","R01 NS099328","NS099328","AARFD-17-529742","1N4R","AG071985"],"pubmed_authors":["Elbatrawy AA","Alnakhala H","Fortin JS","Perry G","Dettmer U","Zhu X","Tripathi A","Plascencia-Villa G","Ademoye TA"],"additional_accession":[]},"is_claimable":false,"name":"Exploring the rhodanine universe: Design and synthesis of fluorescent rhodanine-based derivatives as anti-fibrillar and anti-oligomer agents against α-synuclein and 2N4R tau.","description":"Tau and α-synuclein (α-syn) are prone-to-aggregate proteins that can be responsible for pathological lesions found in the brains of Alzheimer's disease (AD), Lewy body dementia (LBD), and Parkinson's disease (PD) patients. The early-stage oligomers and protofibrils of tau are believed to be strongly linked to human cognitive impairment while the toxic α-syn oligomers are associated with behavioral motor deficits. Therefore, concurrent targeting of both proteinaceous aggregates and oligomers are very challenging. Herein, rhodanine-based compounds were designed and synthesized to target the fibrils and oligomers of tau and α-syn proteins. In particular, the indole-containing rhodanines 5l and 5r displayed significantly high anti-aggregation activity towards α-syn fibrils by reducing of the t","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Dec","modification":"2025-04-04T09:13:01.038Z","creation":"2025-04-04T09:13:01.038Z"},"accession":"S-EPMC11645236","cross_references":{"pubmed":["39550891"],"doi":["10.1016/j.bmc.2024.117990"]}}