Coglitore Diego, Coulon Pierre Eugene, Janot Jean-Marc, Balme Sébastien
Institut Européen des Membranes, UMR5635, Université de Montpellier CNRS ENSCM, Place Eugène Bataillon, 34090 Montpellier, France.
Laboratoire des Solides Irradiés, École polytechnique, Université Paris-Saclay, Route de Saclay, 91128 Palaiseau CEDEX, France.
Materials (Basel). 2019 Oct 28;12(21):3524. doi: 10.3390/ma12213524.
Protein adsorption at the liquid-solid interface is an old but not totally solved topic. One challenge is to find an easy way to characterize the protein behavior on nanoparticles and make a correlation with its intrinsic properties. This work aims to investigate protein adsorption on gold nanoparticles and the colloidal properties. The protein panel was chosen from different structural categories (mainly-α, mainly-β or mix-αβ). The result shows that the colloidal stability with salt addition does not depend on the structural category. Conversely, using the single nanopore technique, we show that the mainly-α proteins form a smaller corona than the mainly-β proteins. We assign these observations to the lower internal energy of α-helices, making them more prone to form a homogeneous corona layer.
蛋白质在液固界面的吸附是一个古老但尚未完全解决的课题。一个挑战是找到一种简便的方法来表征蛋白质在纳米颗粒上的行为，并将其与蛋白质的内在特性建立关联。这项工作旨在研究蛋白质在金纳米颗粒上的吸附及其胶体性质。蛋白质样本选自不同的结构类别（主要为α结构、主要为β结构或αβ混合结构）。结果表明，添加盐后的胶体稳定性并不取决于结构类别。相反，通过单纳米孔技术，我们发现主要为α结构的蛋白质形成的冠层比主要为β结构的蛋白质形成的冠层更小。我们将这些观察结果归因于α螺旋较低的内能，这使得它们更易于形成均匀的冠层。
