Publication | Closed Access
Gallic acid loaded onto polyethylenimine-coated human serum albumin nanoparticles (PEI-HSA-GA NPs) stabilizes α-synuclein in the unfolded conformation and inhibits aggregation
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Citations
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References
2016
Year
NanoparticlesMolecular BiologyNeurochemical BiomarkersSynaptic SignalingSocial SciencesProtein NanoparticlesPei-hsa-ga NpsDifferent Neurodegenerative DisordersNeurobiology Of DiseaseProtein FoldingSynaptic NeuroscienceUnfolded ConformationDegenerative PathologyProtein MisfoldingNeurologyNeuropathologyBiophysicsBiochemistry140-Residue Protein α-SynucleinMajor RoleGallic AcidNeurodegenerationNeurodegenerative DiseasesProteinopathiesDegenerative DiseaseNano-drug DeliveryMedicine
The aggregation of the 140-residue protein α-synuclein (αSN) plays a major role in the pathogenesis of different neurodegenerative disorders such as Parkinson's Disease (PD).
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