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• W2317383762 endingPage "1137" @default.
• W2317383762 startingPage "1131" @default.
• W2317383762 abstract "Inhibition of α-synuclein (ASN) fibril formation is a potential therapeutic strategy in Parkinson's disease and other synucleinopathies. The aim of this study was to examine the role of viologen-phosphorus dendrimers in the α-synuclein fibrillation process and to assess the structural changes in α-synuclein under the influence of dendrimers. ASN interactions with phosphonate and pegylated surface-reactive viologen-phosphorus dendrimers were examined by measuring the zeta potential, which allowed determining the number of dendrimer molecules that bind to the ASN molecule. The fibrillation kinetics and the structural changes were examined using ThT fluorescence and CD spectroscopy. Depending on the concentration of the used dendrimer and the nature of the reactive groups located on the surface, ASN fibrillation kinetics can be significantly reduced, and even, in the specific case of phosphonate dendrimers, the fibrillation can be totally inhibited at low concentrations. The presented results indicate that viologen-phosphorus dendrimers are able to inhibit ASN fibril formation and may be used as fibrillar regulating agents in neurodegenerative disorders." @default.
• W2317383762 created "2016-06-24" @default.
• W2317383762 creator A5011936309 @default.
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• W2317383762 date "2013-02-19" @default.
• W2317383762 modified "2023-10-10" @default.
• W2317383762 title "Viologen-Phosphorus Dendrimers Inhibit α-Synuclein Fibrillation" @default.
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• W2317383762 doi "https://doi.org/10.1021/mp300636h" @default.
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• W2317383762 hasPublicationYear "2013" @default.
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