Abstract: The abnormal aggregation of α-synuclein plays an essential role in the  Parkinson’s disease. A recent study demonstrates the α-synuclein may interact with many different proteins such as A-β peptide and β-synuclein. A-β peptide promotes abnormal aggregation of α-synuclein. However, β-synuclein is resistant to α-synuclein accumulation. The mechanism of promotion or inhibition of the aggregation is not yet clear. We simulate the interaction of α-synuclein with A-β peptide and β-synuclein, and predict the interaction binding sites. The paper provides theoretical evidence for further research of abnormal aggregation.

Key words: β-synuclein,

α-synuclein, A-&beta, active site, homology modeling, molecule docking, peptide