咖啡环效应探测的纳米颗粒上的蛋白质吸附和重组：在单点突变检测中的应用,Journal of the American Chemical Society

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咖啡环效应探测的纳米颗粒上的蛋白质吸附和重组：在单点突变检测中的应用
Journal of the American Chemical Society ( IF 14.4 ) Pub Date : 2016-09-02 , DOI: 10.1021/jacs.6b04833
Stéphanie Devineau _{1,

2} , Manos Anyfantakis _{1,

2} , Laurent Marichal ₃ , Laurent Kiger ₄ , Mathieu Morel _{1,

2} , Sergii Rudiuk _{1,

2} , Damien Baigl _{1,

2}

Affiliation

咖啡环效应表示颗粒在固定在基板上的蒸发固着液滴的边缘处积聚。由于它可以通过简单的目视检查来检测，因此可以将这种普遍存在的现象设想为一种强大且具有成本效益的诊断工具。朝着这个方向，我们在这里系统地分析了含有不同表面特性的聚苯乙烯颗粒和各种蛋白质（牛血清白蛋白 (BSA) 和不同形式的血红蛋白）的干燥液滴的沉积形态。我们表明，沉积模式揭示了蛋白质在颗粒上的吸附及其吸附后重组的信息。通过将模式分析与吸附等温线和 zeta 电位测量相结合，我们表明，咖啡环效应的抑制和盘状图案的形成主要与蛋白质吸附的颗粒中和有关。然而，我们的研究结果还表明，吸附后的蛋白质重组可以显着逆转这种趋势。疏水（分别带电）残基的暴露可导致独立于全局粒子电荷的圆盘（分别为环）沉积物形态。蒸发液滴的表面张力测量和显微镜观察表明，沉积物形态的决定因素是蒸发过程中颗粒在液体/气体界面处的积累。这种一般行为开启了通过分析沉积模式来探测颗粒上蛋白质吸附和重组的可能性，圆盘的形成是通过蛋白质吸附呈现疏水性的颗粒的强大特征。我们表明，这种方法足够灵敏，可以检测蛋白质中的单点突变，正如这里由人类天然血红蛋白 h-HbA 及其突变形式 h-HbS 形成的不同模式所证明的，后者是镰状细胞性贫血的原因。

"点击查看英文标题和摘要"

Protein Adsorption and Reorganization on Nanoparticles Probed by the Coffee-Ring Effect: Application to Single Point Mutation Detection

The coffee-ring effect denotes the accumulation of particles at the edge of an evaporating sessile drop pinned on a substrate. Because it can be detected by simple visual inspection, this ubiquitous phenomenon can be envisioned as a robust and cost-effective diagnostic tool. Toward this direction, here we systematically analyze the deposit morphology of drying drops containing polystyrene particles of different surface properties with various proteins (bovine serum albumin (BSA) and different forms of hemoglobin). We show that deposit patterns reveal information on both the adsorption of proteins onto particles and their reorganization following adsorption. By combining pattern analysis with adsorption isotherm and zeta potential measurements, we show that the suppression of the coffee-ring effect and the formation of a disk-shaped pattern is primarily associated with particle neutralization by protein adsorption. However, our findings also suggest that protein reorganization following adsorption can dramatically invert this tendency. Exposure of hydrophobic (respectively charged) residues can lead to disk (respectively ring) deposit morphologies independently of the global particle charge. Surface tension measurements and microscopic observations of the evaporating drops show that the determinant factor of the deposit morphology is the accumulation of particles at the liquid/gas interface during evaporation. This general behavior opens the possibility to probe protein adsorption and reorganization on particles by the analysis of the deposit patterns, the formation of a disk being the robust signature of particles rendered hydrophobic by protein adsorption. We show that this method is sensitive enough to detect a single point mutation in a protein, as demonstrated here by the distinct patterns formed by human native hemoglobin h-HbA and its mutant form h-HbS, which is responsible for sickle cell anemia.

更新日期：2016-09-02

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