Freie Universität Berlin, Institute of Chemistry & Biochemistry, Takustr. 3, 14195 Berlin, Germany.
Helmholtz Virtual Institute 'Multifunctional Biomaterials for Medicine,' Kantstr. 55, 14513 Teltow, Germany.
Nanomedicine (Lond). 2018 Oct;13(20):2657-2668. doi: 10.2217/nnm-2018-0217. Epub 2018 Oct 18.
We analyzed the protein corona of thermoresponsive, poly(N-isopropylacrylamide)- or poly(N-isopropylmethacrylamide)-based nanogels.
MATERIALS & METHODS: Traces of protein corona detected after incubation in human serum were characterized by proteomics and dynamic light scattering in undiluted serum.
Apolipoprotein B-100 and albumin were the main components of the protein coronae. For dendritic polyglycerol-poly(N-isopropylacrylamide) nanogels at 37°C, an increase in adsorbed immunoglobulin light chains was detected, followed by partially reversible nanogel aggregation. All nanogels in their hydrophilic state are colloidally stable in serum and bear a dysopsonin-rich protein corona.
We observed strong changes in NG stability upon slight alterations in the composition of the protein coronae according to nanogel solvation state. Nanogels in their hydrophilic state possess safe protein coronae.
我们分析了温敏型聚（N-异丙基丙烯酰胺）或聚（N-异丙基甲基丙烯酰胺）纳米凝胶的蛋白质冠。
在人血清中孵育后检测到的蛋白质冠的痕迹，通过蛋白质组学和未稀释血清中的动态光散射进行了表征。
载脂蛋白 B-100 和白蛋白是蛋白质冠的主要成分。对于 37°C 的树枝状聚甘油-聚（N-异丙基丙烯酰胺）纳米凝胶，检测到吸附的免疫球蛋白轻链增加，随后纳米凝胶部分可逆聚集。所有在亲水性状态下的纳米凝胶在血清中均具有胶体稳定性，并带有富含调理素的蛋白质冠。
我们观察到，根据纳米凝胶的溶剂化状态，蛋白质冠组成的微小变化会导致 NG 稳定性发生强烈变化。处于亲水性状态的纳米凝胶具有安全的蛋白质冠。
