Abstract
AbstractMisfolded protein formation and aggregation are the central hallmarks for various neurodegenerative disorders. When it comes to Parkinson's disease (PD), alpha‐synuclein (α‐syn) is the culprit protein. The presence of α‐syn protein in lewy bodies and lewy neurites confirmed its presence in the occurrence of PD. The protein is natively present in the soluble monomeric forms, but certain factors such as oxidative stress convert the structure into insoluble oligomeric formats. This study focuses on the inhibitory effects of various antioxidant compounds on α‐syn oligomerization. We had collected the list of compounds present in the Camellia sp. plant. Using a computational approach, we found the potential interaction sites between the antioxidant compounds and α‐syn using a computational approach. Molecular docking and simulation studies suggest that the compound Theaflavin‐3‐3‐digallate shows best interactions with −7.1 kcal/mol and can reduce the alpha‐sheet structure of α‐syn structure to loop region.
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