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首页> 外文期刊>Applied Surface Science >Adsorption of intrinsically disordered barnacle adhesive proteins on silica surface
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Adsorption of intrinsically disordered barnacle adhesive proteins on silica surface

机译：固有紊乱的藤壶黏附蛋白在二氧化硅表面的吸附

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The adsorption of recombinant barnacle proteins Bacp19k and Mrcp19k on hydrophilic silica surface was characterized by spectroscopic ellipsometry in artificial seawater (pH = 8.2). They are homologous adhesive proteins destined for underwater adhesion but bear opposite net charges in seawater. As assessed with their primary and secondary structures, both proteins are intrinsically disordered and thus distinct from globular proteins that have dominated research in the field. Different from Mrcp19k, higher initial rate and adsorbed amount were obtained via curve fitting for Bacp19k in kinetic studies, due to favorable charge interactions with silica surface. The good fitting with the same dynamic model also indicates the formation of monolayer coverage in both cases. The two adsorption isotherms of Bacp19k and Mrcp19k are different in the initial change and maximum adsorption level, indicating different protein-surface affinities and charge interactions. Each isotherm fits the Langmuir model well, which is commonly used to describe monolayer adsorption, thus consistent with the predication from kinetic fitting. To further examine the effect of electrostatic interaction on the adsorption, the isotherm of the 1: 1 mixture of Bacp19k and Mrcp19k was also constructed, which showed a higher correlation fit for Jovanovic than for Langmuir model. The presence of electrostatic attraction between Bacp19k and Mrcp19k deviated from one of the required conditions for Langmuir behavior, which may also result in the highest coadsorption level but slowest initial change among the three isotherms. The surface state of the adhesive proteins and the change with adsorption time were also examined by atomic force microscopy. The results thus obtained are in good agreement with the corresponding ellipsometric measurement. (C) 2017 Elsevier B.V. All rights reserved.
机译：重组藤壶蛋白Bacp19k和Mrcp19k在亲水性二氧化硅表面的吸附通过分光镜椭圆偏振法在人工海水（pH = 8.2）中表征。它们是注定要在水下粘附的同源粘附蛋白，但在海水中却带有相反的净电荷。根据其一级和二级结构评估，这两种蛋白本质上都是无序的，因此与在该领域占据主导地位的球形蛋白不同。与Mrcp19k不同，动力学研究中通过曲线拟合获得Bacp19k的初始速率和吸附量较高，这是由于与二氧化硅表面的电荷相互作用良好。具有相同动态模型的良好拟合也表明在两种情况下均形成了单层覆盖。 Bacp19k和Mrcp19k的两个吸附等温线在初始变化和最大吸附水平上不同，表明不同的蛋白质表面亲和力和电荷相互作用。每个等温线都很好地拟合了Langmuir模型，该模型通常用于描述单层吸附，因此与动力学拟合的预测一致。为了进一步检查静电相互作用对吸附的影响，还构建了Bacp19k和Mrcp19k的1：1混合物的等温线，与Johanovic模型相比，Jovanovic模型的相关拟合更高。 Bacp19k和Mrcp19k之间静电吸引的存在偏离了Langmuir行为的必要条件之一，这也可能导致最高的共吸附水平，但三个等温线中的初始变化最慢。还通过原子力显微镜检查了粘附蛋白的表面状态和随吸附时间的变化。如此获得的结果与相应的椭偏测量值非常吻合。 （C）2017 Elsevier B.V.保留所有权利。

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