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首页> 外文期刊>Nanotechnology >Effects of the dielectric properties of the ceramic-solvent interface on the binding of proteins to oxide ceramics: a non-local electrostatic approach
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Effects of the dielectric properties of the ceramic-solvent interface on the binding of proteins to oxide ceramics: a non-local electrostatic approach

机译：陶瓷溶剂界面介电性能对氧化物陶瓷蛋白质结合的影响：非局部静电方法

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The rapid development of nanoscience and nanotechnology has raised many fundamental questions that significantly impede progress in these fields. In particular, understanding the physicochemical processes at the interface in aqueous solvents requires the development and application of efficient and accurate methods. In the present work we evaluate the electrostatic contribution to the energy of model protein-ceramic complex formation in an aqueous solvent. We apply a non-local (NL) electrostatic approach that accounts for the effects of the short-range structure of the solvent on the electrostatic interactions of the interfacial systems. In this approach the aqueous solvent is considered as a non-ionic liquid, with the rigid and strongly correlated dipoles of the water molecules. We have found that an ordered interfacial aqueous solvent layer at the protein- and ceramic-solvent interfaces reduces the charging energy of both the ceramic and the protein in the solvent, and significantly increases the electrostatic contribution to their association into a complex. This contribution in the presented NL approach was found to be significantly shifted with respect to the classical model at any dielectric constant value of the ceramics. This implies a significant increase of the adsorption energy in the protein-ceramic complex formation for any ceramic material. We show that for several biocompatible ceramics (for example HfO2, ZrO2, and Ta2O5) the above effect predicts electrostatically induced protein- ceramic complex formation. However, in the framework of the classical continuum electrostatic model (the aqueous solvent as a uniform dielectric medium with a high dielectric constant similar to 80) the above ceramics cannot be considered as suitable for electrostatically induced complex formation. Our results also show that the protein- ceramic electrostatic interactions can be strong enough to compensate for the unfavorable desolvation effect in the process of protein-ceramic complex formation.
机译：纳米科学和纳米技术的快速发展提出了许多基本问题，这显着妨碍了这些领域的进展。特别地，了解含水溶剂中的界面中的物理化学方法需要开发和应用有效和准确的方法。在本工作中，我们评估水性溶剂中模型蛋白质 - 陶瓷复合物的能量的静电贡献。我们应用非局部（NL）静电方法，该方法考虑溶剂对界面系统的静电相互作用的影响。在这种方法中，水性溶剂被认为是非离子液体，具有刚性和强烈相关的水分子的偶极子。我们发现蛋白质和陶瓷 - 溶剂界面处的有序界面水性溶剂层降低了陶瓷和蛋白质中的溶剂中的充电能量，并显着提高了它们与其结合的静电贡献。发现所呈现的NL方法中的这种贡献被发现在陶瓷的任何介电常数值下都是显着的。这意味着任何陶瓷材料蛋白质 - 陶瓷复合物形成中吸附能量的显着增加。我们表明，对于几种生物相容性陶瓷（例如HFO2，ZrO2和Ta2O5），上述效果预测静电诱导的蛋白质陶瓷复合物形成。然而，在经典连续静脉静电模型的框架中（作为具有高介电常数的均匀介电介质的水性溶剂类似于80），不能认为上述陶瓷是适合于静电诱导的复杂形成。我们的研究结果还表明，蛋白质陶瓷静电相互作用足以满足蛋白质 - 陶瓷复合物形成过程中不利的脱溶解效果。

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