LilrB2蛋白与Aβ(1-42)寡聚态的结合会造成阿尔茨海默症的某些症状，研究其中的结合方式对设计针对性抑制剂具有重要意义。以lilrB2蛋白和Aβ(16-21)双分子链为研究对象，通过分子对接设定3个不同构象作为分子动力学模拟起点，分析3组体系的模拟轨迹，发现lilrB2蛋白上的ASP23残基与Aβ(16-21)单支链上的LYS残基有较强的相互作用，对受体和配体结合起到了重要的影响。在不同结合状态下，lilrB2蛋白的CYS142和SER24残基与Aβ(16-21)支链上VAL、PHE和ALA残基的疏水作用也有利于lilrB2蛋白和Aβ(16-21)双分子链的结合。
LilrB2 is a kind of protein targeted by Aβ (1-42) oligomers. The binding of them may result in some symptoms related to Alzheimer’s disease. It’s important to explore the binding mechanisms for the design of inhibitors. Three different conformations were designed by molecular docking of lilrB2 and double-stranded Aβ (16-21), and were used as the initial conformations for molecular dynamics simulations. Three sets of data were analyzed, finding that the ASP23 residue on lilrB2 had a strong interaction with LYS residue on the chain of Aβ (16-21), which had an obvious effect on the binding of receptor and ligand. In different binding states, the interaction of CYS142 residue with VAL or PHE on the chain of Aβ (16-21) and the interaction of SER24 residue with ALA on the chain of Aβ (16-21) are favorable for the binding of receptor and ligand.
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