Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany.
Consiglio Nazionale delle Ricerche (Instituto Officina dei Materiali) and INSIDE@ILL c/o Institut Laue-Langevin, 38042 Grenoble, France.
Biomacromolecules. 2022 Oct 10;23(10):4282-4288. doi: 10.1021/acs.biomac.2c00744. Epub 2022 Sep 9.
When in contact with a biological medium, the surfaces of nanoparticles are usually covered by proteins. In this regard, it was found that poly(ethylene glycol) (PEG) promotes the "stealth effect". This implies a reduction of unspecific protein adsorption and cellular uptake. Although information about the PEG-protein interaction was reported, more accurate and sophisticated structure and dynamics analyses are needed to understand the interaction processes in detail. This work studies the PEG-protein interaction using model nanoparticles stabilized either by the PEG-based surfactant Lutensol AT50 or sodium dodecyl sulfate. The interaction with human serum albumin was studied using neutron scattering techniques. The parameters obtained by small-angle neutron scattering yielded information about the adsorbed protein layer thickness. Protein structure changes were detected via differential scanning fluorimetry and elastic neutron scattering. This combination gives a better insight into the PEG-protein interaction, contributing to the design of nanomaterials for medical applications.
当与生物介质接触时，纳米粒子的表面通常会被蛋白质覆盖。在这方面，人们发现聚乙二醇（PEG）促进了“隐身效应”。这意味着减少了非特异性蛋白质吸附和细胞摄取。尽管已经报道了有关 PEG-蛋白质相互作用的信息，但需要更准确和复杂的结构和动力学分析来详细了解相互作用过程。本工作使用基于 PEG 的表面活性剂 Lutensol AT50 或十二烷基硫酸钠稳定的模型纳米粒子研究了 PEG-蛋白质相互作用。使用中子散射技术研究了与人血清白蛋白的相互作用。小角中子散射获得的参数提供了有关吸附蛋白质层厚度的信息。通过差示扫描荧光法和弹性中子散射检测到蛋白质结构的变化。这种组合可以更好地了解 PEG-蛋白质相互作用，有助于为医学应用设计纳米材料。
