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Fig. 3 | Molecular Neurodegeneration

Fig. 3

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

Fig. 3

Analysis of NPH CSF samples. A Protein aggregation assay performed using 0.7 mg/mL of recombinant α-syn in PBS with 40 μl of CSF from 2 NPH subjects (40 µL). The two ThT fluorescence traces are represented as average intensity over 3 replicates with error bars representing the SEM. B Portion of 1D 1H NMR spectra relative to the two NPH CSF samples. C Relative concentration (emPAI score multiplied by protein molecular weight) ratio of total protein and the three most abundant protein constituents measured by nLC-nESI HRMS/MS in neat NPH1 and NPH2 CSF samples. Approximately 200 and 400 different proteins were detected in NPH1 and NPH2, respectively. Albumin was the most abundant protein followed by apolipoproteins and complement proteins. Apolipoproteins scores were summed together, with ApoA1 and ApoE being the most abundant (~ 85% of the total). Complement C3 and C4 were found as the most abundant complement proteins (~ 65% of the total)

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Molecular Neurodegeneration

ISSN: 1750-1326