Loss in Toxic Function of Aggregates of α-Synuclein Mutants by a β-Synuclein Derived Peptide

Soheila Mohammadi, Maryam Nikkhah, Saman Hosseinkhani
  • Protein and Peptide Letters, October 2017, Bentham Science Publishers
  • DOI: 10.2174/0929866524666170818154033

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.

Perspectives

Soheila Mohammadi
Tarbiat Modares University

It can help researchers working on inhibiting αS mutants.

Read Publication

http://dx.doi.org/10.2174/0929866524666170818154033

The following have contributed to this page: Professor Saman Hosseinkhani and Soheila Mohammadi