Rational Design of Small-Molecule Stabilizers for Human FAH Protein

Riccardo Scarin published a dataset on figshare in May 2026 describing small-molecule pharmacological chaperones for the human fumarylacetoacetate hydrolase (FAH) protein. The data likely contains results from an integrated workflow including X-ray structures, NMR, isothermal titration calorimetry, DOSY-NMR, circular dichroism, and activity assays. The compounds were validated in CRISPR-engineered cellular models and a mouse model of hereditary tyrosinemia type 1.

Use Cases

• Train machine learning models for binding affinity prediction based on low-μM affinity measurements.
• Analyze structure-activity relationships for pharmacological chaperones based on X-ray structural data.
• Validate protein stabilization predictions using NMR and circular dichroism data.
• Benchmark compound efficacy in cellular models based on CRISPR-engineered validation data.
• Assess dose-dependent functional effects based on FAH activity assay results.

Strengths

• Data is derived from an integrated workflow guided by X-ray structures of human FAH.
• Compounds were validated by multiple biophysical techniques (NMR, ITC, DOSY-NMR, CD).
• Functional effects were tested in cellular and animal models (CRISPR-engineered cells, mouse model).

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.
• Dataset size is 1.0 KB, indicating a very limited scope, likely containing summary or metadata rather than raw experimental data.

Provenance

Source

figshare

Collection Method

Integrated workflow guided by X-ray structures, validated by biophysical and functional assays.

Freshness

Last updated 2026-05-12 10:32:24.