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  11. Allium Sativum-derived Alliin And Allicin Stably Bind To Α-synuclein And Prevent Its Cytotoxic Aggregation

Allium sativum-Derived Alliin and Allicin Stably Bind to α-Synuclein and Prevent Its Cytotoxic Aggregation

S Rehan Ahmad1, Md Zeyaullah2, Abdullah M AlShahrani2

  • 1Hiralal Mazumdar Memorial College for Women, West Bengal State University, Kolkata, West Bengal, India.

Proteins
|June 14, 2025

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View abstract on PubMed

Summary
This summary is machine-generated.

Compounds from garlic, including alliin and allicin, show promise in inhibiting alpha-synuclein aggregation, a key factor in Parkinson's disease, offering potential neuroprotective effects.

Area of Science:

  • Neuroscience
  • Pharmacology
  • Biochemistry

Background:

  • Neurodegenerative diseases like Parkinson's involve pathological alpha-synuclein aggregation.
  • Natural compounds offer a therapeutic avenue for targeting this aggregation.

Purpose of the Study:

  • To evaluate sulfur-containing compounds from Allium sativum for their potential to inhibit alpha-synuclein aggregation.
  • To assess drug-likeness, pharmacokinetic properties, and neuroprotective effects of these compounds.

Main Methods:

  • In silico analysis including ADMET profiling, molecular docking, molecular dynamics simulations, and MM-GBSA binding energy calculations.
  • In vitro validation using SH-SY5Y cell-based models for alpha-synuclein aggregation and cytotoxicity assays.

Main Results:

Keywords:
alliin and allicinneuroprotectionparkinson's diseasephyto‐bioactive compounds

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  • Nine compounds exhibited good gastrointestinal absorption; six were predicted to cross the blood-brain barrier.
  • Alliin, allicin, E-ajoene, and diallyl disulfide showed strong binding to alpha-synuclein.
  • Alliin and allicin demonstrated significant reduction in alpha-synuclein aggregation and cytotoxicity in cellular assays.

Conclusions:

  • Allium sativum-derived compounds, particularly alliin and allicin, are promising lead candidates for therapeutic intervention in alpha-synucleinopathies.
  • These compounds effectively inhibit alpha-synuclein aggregation and mitigate associated neurotoxicity.
α‐synuclein aggregation