S129 α-Synuclein Mutant Effects on Structure, Aggregation, and Neurotoxicity

Experimental data on two artificial single point mutations (S129A and S129W) of the α-synuclein protein, compared to the wild-type. The dataset includes results from Circular Dichroism and Raman spectroscopy for secondary structure, Thioflavin T assays and atomic force microscopy for aggregation kinetics, and cytotoxicity tests on SH-SY5Y neuronal cell lines. It was authored by Esha Pandit and last updated on 2026-06-03.

Use Cases

• Compare secondary structure propensity (α-helical vs. β-sheet) based on Circular Dichroism and Raman spectroscopy data
• Analyze aggregation kinetics and fibril formation lag phases based on Thioflavin T assay results
• Assess relative cytotoxicity of protein oligomers based on cell survivability rates from SH-SY5Y neuronal cell line tests
• Investigate the relationship between protein structural stability and neurotoxicity based on the described experimental findings

Strengths

• Includes specific quantitative results, such as cell survivability rates of ~40% for wild-type oligomers and ~80% for mutant oligomers
• Covers multiple experimental modalities: spectroscopy, aggregation assays, microscopy, and cytotoxicity tests
• Data is licensed under CC-BY-4.0, permitting open sharing and adaptation

Limitations

• Column-level documentation is absent; field semantics must be inferred after download
• Row count is unknown, which may limit suitability assessment
• The primary data file is a 1.8 MB DOCX document, which may require parsing to extract structured data

Provenance

Source

figshare

Collection Method

Experimental laboratory study using spectroscopy, microscopy, and cell culture assays.

Freshness

Last updated 2026-06-03 14:41:04; freshness should be verified