The effect of a β-Synuclein Derived Peptide on Aggregates of α -Synuclein Mutants
What is it about?
The neuropathological hallmark of Parkinson’s disease (PD) is the presence of protein inclusions of α-Synuclein (αS) within the surviving neurons. In this work, we aimed to investigate the effects of a β-Synuclein derived peptide on oligomerization of pathological mutants of αS (A53T, A30P, E46K) by fluorescence spectroscopy and electron microscopy. The influence of the peptide inhibitor on cell toxicity of aggregation products of αS and its mutants were investigated by MTT assay and flow cytometry.
Why is it important?
We shown that the peptide inhibitor effectively blocks the fibrillation of not only the native αS but also the PD related αS mutants in vitro, suggesting a similar mechanism of oligomerization for native and mutants of αS. Our study proved the broadness of a peptides inhibitory effects, suggesting a similar mechanism of oligomerization for native and mutants of αS.
The following have contributed to this page: Professor Saman Hosseinkhani and Soheila Mohammadi
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