温度诱导的BSA蛋白分子变性以改善表面钝化涂层,ACS Applied Materials & Interfaces

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温度诱导的BSA蛋白分子变性以改善表面钝化涂层
ACS Applied Materials & Interfaces ( IF 8.3 ) Pub Date : 2018-09-04 00:00:00 , DOI: 10.1021/acsami.8b13749
Jae Hyeon Park ₁ , Joshua A. Jackman ₁ , Abdul Rahim Ferhan ₁ , Gamaliel Junren Ma ₁ , Bo Kyeong Yoon ₁ , Nam-Joon Cho _{1,

2}

Affiliation

牛血清白蛋白（BSA）是最广泛用于表面钝化应用的蛋白质，尽管它与亲水性表面（如二氧化硅基材料）具有相对较弱的非粘性相互作用。在本文中，我们报告了一种简单而通用的方法来增加BSA蛋白分子吸附到二氧化硅表面上的粘性，从而使针对血清生物污染的阻断效率提高多达10倍。圆二色光谱，动态光散射和纳米颗粒跟踪分析表明，温度诱导的BSA蛋白质在本体溶液中的变性导致不可逆的展开和蛋白质寡聚，从而将粘附力弱的蛋白质单体转化为粘附力更强的寡聚形式。冷却后，经热处理的变性BSA低聚物保持稳定。室温石英微平衡耗散和局部表面等离子体共振实验表明，变性的BSA低聚物比天然BSA单体更快，更大量地吸附到二氧化硅表面。我们还确定，变性的BSA低聚物的较大的表面接触面积是导致其更具粘合性的重要因素。重要的是，变性的BSA低聚物是一种优异的钝化剂，可抑制二氧化硅表面的生物结垢，并改善Western blot应用性能。综上所述，这些发现证明了温度诱导的BSA蛋白分子变性如何能够导致用于表面钝化应用的改进的基于蛋白质的涂层。

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Temperature-Induced Denaturation of BSA Protein Molecules for Improved Surface Passivation Coatings

Bovine serum albumin (BSA) is the most widely used protein for surface passivation applications, although it has relatively weak, nonsticky interactions with hydrophilic surfaces such as silica-based materials. Herein, we report a simple and versatile method to increase the stickiness of BSA protein molecules adsorbing onto silica surfaces, resulting in up to a 10-fold improvement in blocking efficiency against serum biofouling. Circular dichroism spectroscopy, dynamic light scattering, and nanoparticle tracking analysis showed that temperature-induced denaturation of BSA proteins in bulk solution resulted in irreversible unfolding and protein oligomerization, thereby converting weakly adhesive protein monomers into a more adhesive oligomeric form. The heat-treated, denatured BSA oligomers remained stable after cooling. Room-temperature quartz crystal microbalance-dissipation and localized surface plasmon resonance experiments revealed that denatured BSA oligomers adsorbed more quickly and in larger mass quantities onto silica surfaces than native BSA monomers. We also determined that the larger surface contact area of denatured BSA oligomers is an important factor contributing to their more adhesive character. Importantly, denatured BSA oligomers were a superior passivating agent to inhibit biofouling on silica surfaces and also improved Western blot application performance. Taken together, the findings demonstrate how temperature-induced denaturation of BSA protein molecules can lead to improved protein-based coatings for surface passivation applications.

更新日期：2018-09-04

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