Parkinson's disease (PD) is a progressive neurodegenerative disorder characterized by motor dysfunction and cognitive decline, primarily attributed to the abnormal accumulation of alpha-synuclein (α-syn). This protein tends to misfold and aggregate, forming Lewy bodies, which are pathological hallmarks of PD. The aggregation of α-syn disrupts neuronal function and viability, leading to the clinical manifestations of the disease. Previous studies have explored interactions between amyloidogenic proteins and S100 family members, suggesting the involvement of S100 proteins, a family of calcium-binding proteins, in neurodegenerative processes. Notably, interactions between S100A9 and α-synuclein have been documented, where S100A9 influences the aggregation kinetics and fibril structure of α-syn, potentially worsening neurodegeneration.