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Fatty acid transfer between serum albumins and shungite carbon nanoparticles and its effect on protein aggregation and association
European Biophysics Journal ( IF 2.2 ) Pub Date : 2019-12-21 , DOI: 10.1007/s00249-019-01414-y
Andrey Goryunov 1 , Sergei Rozhkov 1 , Natalia Rozhkova 2
Affiliation  

Abstract

The bioactivity of the natural ultrafine carbon form shungite nanocarbon (ShC) is of particular interest both for biomedical applications of such nanomaterials and their negative impact on the aquatic environmental. Here we studied the interaction of serum albumin (SA) with ShC nanoparticles in aqueous dispersion with respect to its structural-dynamic, thermodynamic, and hydrodynamic effects. Electron spin resonance (EPR) with a 5-DOXYL-stearic acid spin probe (5DSA) demonstrates that ShC can affect fatty acid (FA) binding by SA, protein conformation in the stearic FA spin probe binding region, and protein aggregation due to the partial transfer of FA to the ShC nanoparticles. The ratio of SA fractions changes in the presence of ShC in favor of the fraction that is less saturated with FA as shown by differential scanning calorimetry (DSC). The stability of interaction with ShC is significantly higher for aggregates of SA molecules that carry physiological amounts of FA, compared to aggregates of the FA-free protein, as studied by dynamic light scattering (DLS) analysis. Generally, the mixed dispersion of SA and ShC nanoparticles is more homogeneous than the SA solution alone. This is manifested both in the size of the molecular associates and in the microenvironment of the protein-bound FA. The formation of the SA–ShC interface is likely to result in a greater uniformity of the FA binding sites and a decrease in protein fractions and "hot patches" on the protein surface responsible for the supramolecular heterogeneity of the protein in solution.



中文翻译:

血清白蛋白与闪石碳纳米颗粒之间的脂肪酸转移及其对蛋白质聚集和缔合的影响

摘要

天然超细碳形式的次石墨纳米碳 (ShC) 的生物活性对于此类纳米材料的生物医学应用及其对水生环境的负面影响都特别令人感兴趣。在这里,我们研究了血清白蛋白 (SA) 与 ShC 纳米粒子在水分散体中的结构动力学、热力学和流体动力学效应的相互作用。带有 5-DOXYL-硬脂酸自旋探针 (5DSA) 的电子自旋共振 (EPR) 表明,ShC 可以影响 SA 对脂肪酸 (FA) 的结合、硬脂酸 FA 自旋探针结合区域中的蛋白质构象以及由于FA 部分转移到 ShC 纳米颗粒。如差示扫描量热法 (DSC) 所示,SA 级分的比率在 ShC 存在下发生变化,有利于 FA 饱和度较低的级分。通过动态光散射 (DLS) 分析研究,与不含 FA 的蛋白质的聚集体相比,携带生理量 FA 的 SA 分子聚集体与 ShC 相互作用的稳定性显着更高。通常,SA 和 ShC 纳米粒子的混合分散体比单独的 SA 溶液更均匀。这体现在分子缔合体的大小和蛋白质结合 FA 的微环境中。SA-ShC 界面的形成可能导致 FA 结合位点的更大均匀性和蛋白质组分的减少和蛋白质表面上导致溶液中蛋白质超分子异质性的“热斑”。通过动态光散射 (DLS) 分析研究,与不含 FA 的蛋白质的聚集体相比。通常,SA 和 ShC 纳米粒子的混合分散体比单独的 SA 溶液更均匀。这体现在分子缔合体的大小和蛋白质结合 FA 的微环境中。SA-ShC 界面的形成可能导致 FA 结合位点的更大均匀性和蛋白质组分的减少和蛋白质表面上导致溶液中蛋白质超分子异质性的“热斑”。与无 FA 蛋白质的聚集体相比,通过动态光散射 (DLS) 分析进行研究。通常,SA 和 ShC 纳米粒子的混合分散体比单独的 SA 溶液更均匀。这体现在分子缔合体的大小和蛋白质结合 FA 的微环境中。SA-ShC 界面的形成可能导致 FA 结合位点的更大均匀性和蛋白质组分的减少和蛋白质表面上导致溶液中蛋白质超分子异质性的“热斑”。这体现在分子缔合体的大小和蛋白质结合 FA 的微环境中。SA-ShC 界面的形成可能导致 FA 结合位点的更大均匀性和蛋白质组分的减少和蛋白质表面上导致溶液中蛋白质超分子异质性的“热斑”。这体现在分子缔合体的大小和蛋白质结合 FA 的微环境中。SA-ShC 界面的形成可能导致 FA 结合位点的更大均匀性和蛋白质组分的减少和蛋白质表面上导致溶液中蛋白质超分子异质性的“热斑”。

更新日期:2020-04-21
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