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首页> 外文期刊>Polymer Preprints >Exploiting silicone-protein interactions: stabilization against denaturation at interfaces
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Exploiting silicone-protein interactions: stabilization against denaturation at interfaces

机译：利用有机硅-蛋白质相互作用：稳定界面抗变性

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摘要

Silicones are exceptionally hydrophobic materials, which is partly the source of their impressive surface activity. By contrast, proteins are generally very hydrophilic, at least at their external surface. Relatively little energy is normally needed to perturb protein tertiary structure. Favorable interactions between the more hydrophobic protein core with silicone oils has been attributed to the facile denaturation that can occur if proteins are exposed to dimethylsilicone fluids (e.g., with emulsification). In such a case, hydrophobic domains on both polymers can associate.
机译：有机硅是非常疏水的材料，部分是其令人印象深刻的表面活性的来源。相反，蛋白质通常至少在其外表面是非常亲水的。通常，扰动蛋白质三级结构所需的能量相对较少。疏水性更高的蛋白质核心与硅油之间的良好相互作用已被归因于蛋白质暴露于二甲基硅氧烷流体（例如，乳化）时可能发生的变性。在这种情况下，两种聚合物上的疏水域都可以缔合。

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