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Molecular dynamics simulations to determine the effect of supercritical carbon dioxide on the structural integrity of hen egg white lysozyme

机译:分子动力学模拟,以确定超临界二氧化碳对鸡蛋清溶菌酶结构完整性的影响

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In this study, various molecular dynamics simulations were conducted to investigate the effect of supercritical carbon dioxide on the structural integrity of hen egg white lysozyme. The analyses of backbone root-mean-square deviation, radius of gyration, and secondary structure stability all show that supercritical CO2 exhibits the ability to increase the stability of this protein, probably as a result of the solvent with less polarity, where hydrophobic interactions stabilizing the native structure are weakened and simultaneously the local hydrogen bonds are strengthened, resulting in stabilization of the secondary structures. The hydrophobic cores in the alpha- and beta-domains also play an important role in preventing this protein from thermal unfolding. As supercritical CO2 has been attractive for biomedical applications because of the advantages of mild critical condition, nonflammability, nontoxity, and the purity of the resulting products, the structural stabilizing effect found in this study strongly suggests that it is possible to increase the thermostability of hen egg white lysozyme by pretreatment with supercritical CO2, leading to better industrial applications of this protein.
机译:在这项研究中,进行了各种分子动力学模拟,以研究超临界二氧化碳对鸡蛋清溶菌酶结构完整性的影响。对骨干均方根偏差,回转半径和二级结构稳定性的分析均表明,超临界CO2能够提高该蛋白的稳定性,这可能是由于极性较小的溶剂所致,疏水作用稳定了天然结构被削弱,同时局部氢键被增强,导致二级结构的稳定。 α-和β-结构域中的疏水核心在防止这种蛋白质热解折叠中也起着重要作用。由于超临界CO2由于温和的临界条件,不易燃,无毒以及所得产品的纯度而对生物医学具有吸引力,因此本研究中发现的结构稳定作用强烈表明可以提高母鸡的热稳定性。蛋清溶菌酶经超临界CO2预处理后,可更好地在工业上应用。

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