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Fig. 6 | Molecular Neurodegeneration

Fig. 6

From: Cerebrospinal fluid lipoproteins inhibit α-synuclein aggregation by interacting with oligomeric species in seed amplification assays

Fig. 6

HDL reduces α-syn aggregation even at CSF physiological (ca. 0.03 mg/mL) and sub-physiological levels by preventing the formation of transient oligomeric/protofibrillary species. A Protein aggregation assay performed using 0.7 mg/mL of recombinant α-syn in PBS with 0, 0.003, 0.03, 0.3 and 1 mg/mL of added human serum HDL. To remove the background fluorescence, the average fluorescence of three replicates containing the same amounts of HDL without α-syn was subtracted prior to the analysis. All ThT fluorescence traces are represented as average intensity over 3 replicates with error bars representing SEM. B The presence of monomeric α-syn (14–18 kDa) in samples collected at different timepoints of the spontaneous aggregation process were monitored by WB using Syn211 antibody. Monomeric α-syn decreases as t increases due to the formation of fibrils. C In a similar way, a WB with Syn211 was performed on the reaction products obtained after 180 h, at different HDL concentrations with and without α-syn

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