SARS冠状病毒主要蛋白酶二聚体静电和疏水效应的研究

从三种冠状病毒主要蛋白酶SARS 3CL, HCoV 3CL和TGEC 3CL蛋白酶结构出发,着重研究了三种蛋白酶二聚体单体之间的静电和疏水相互作用.用连续介质模型有限差分方法计算得到三种蛋白二聚体界面处的静电势,发现三种蛋白酶单体和单体之间静电势分布具有明显的互补性,三种蛋白酶二聚体单体之间具有相同的静电相互作用能.用溶剂可及表面积模型分析了分子表面积及疏水性,发现三种蛋白酶具有相同的疏水分布,其中SARS 3CL蛋白酶疏水率为74%,驱动其单体聚合成二聚体.对三种蛋白酶的去溶剂化能疏水项的计算表明,三种蛋白酶二聚体单体之间具有相似的疏水相互作用能.

Electrostatic and Hydrophobic Interactions in SARS Coronavirus Main Proteinase Dimer

The crystal structures of the three coronavirus main proteinases, SARS 3CL, HCoV 3CL and TGEV 3CL, are used to study the electrostatic and hydrophobic interactions between two monomers. The continuum model and the finite difference Poisson-Boltzmann (FDPB) method were used to calculate the electrostatic potentials on the interface of the three dimers. In each dimer, the two monomers exhibit apparent electrostatic complementarity and the electrostatic interaction energies are very similar among the dimers. The solvent accessible surface model was applied for the molecular surface and hydrophobicity. The hydrophobic distributions were similar for the three proteinases. Seventy-four percent area of SARS 3CL proteinase surface is hydrophobic which is the main drive of dimer formation. The similar hydrophobic desolvation free energies indicate that electrostatic interaction energies are very similar among the three coronavirus main proteinase dimers.