α-synuclein蛋白与A-β肽和β-synuclein蛋白相互作用位点的预测

摘要

α-synuclein蛋白的异常聚集是引起帕金森病的重要因素.实验研究发现,α-synuclein蛋白能与多个蛋白相互作用.在相互作用的蛋白质中,有的可以促进α-synuclein的异常聚集,如A-β肽；有的可以抑制α-synuclein的异常聚集,如β-synuclein蛋白,但促进或抑制α-synuclein异常聚集的机理并不明确.利用SYBYL和AUTODOK软件模拟α-synuclein蛋白与A-β肽和β-synuclein的相互作用,找到其相互作用位点,为进一步研究α-synuclein蛋白的异常聚集提供理论依据.%The abnormal aggregation of a-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 p-synuclein, and predict the interaction binding sites. The paper provides theoretical evidence for further research of abnormal aggregation.