Abstract
Parkinson's disease (PD), closely associated with the misfolding and aggregation of the neuronal protein α-synuclein (A-Syn), is a neurodegenerative disorder with no cure to date. Here, we show that the commercially available, inexpensive, aminoglycoside antibiotic kanamycin effectively inhibits both lipid-induced and solution-phase aggregation of A-Syn in vitro, pointing towards the prospective repurposing of kanamycin as a potential anti-PD drug.
MeSH terms
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Anti-Bacterial Agents / chemistry
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Anti-Bacterial Agents / metabolism
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Anti-Bacterial Agents / pharmacology*
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Cell Line, Tumor
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Humans
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Kanamycin / chemistry
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Kanamycin / metabolism
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Kanamycin / pharmacology*
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Phosphatidylcholines / chemistry
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Phosphatidylethanolamines / chemistry
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Phosphatidylserines / chemistry
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Protein Binding / drug effects
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Protein Conformation / drug effects
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Protein Multimerization / drug effects*
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Unilamellar Liposomes / chemistry
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Unilamellar Liposomes / metabolism
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alpha-Synuclein / metabolism*
Substances
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Anti-Bacterial Agents
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Phosphatidylcholines
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Phosphatidylethanolamines
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Phosphatidylserines
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Unilamellar Liposomes
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alpha-Synuclein
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Kanamycin
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1,2-dioleoylphosphatidylserine
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1,2-dielaidoylphosphatidylethanolamine
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1,2-oleoylphosphatidylcholine