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Impact of oppositely charged shell and cores on interaction of core-shell colloids with differently charged proteins as a route for tuning of the colloids cytotoxicity.
Colloids and Surfaces B: Biointerfaces ( IF 5.8 ) Pub Date : 2020-08-05 , DOI: 10.1016/j.colsurfb.2020.111306
Julia Elistratova 1 , Bulat Faizullin 2 , Igor Strelnik 1 , Tatiana Gerasimova 1 , Rafil Khairullin 2 , Anastasiia Sapunova 1 , Alexandra Voloshina 1 , Timur Mukhametzyanov 2 , Elvira Musina 1 , Andrey Karasik 1 , Asiya Mustafina 1
Affiliation  

The present work represents interactions between the core-shell nanoparticles and different proteins, exemplified by lysozyme (LSZ), pepsin, bovine serum albumin (BSA), thioredoxin (TRX) and yellow fluorescent protein (YFP). The core-shell morphology derives from the non-covalent deposition of polyethyleneimine (PEI) onto nanoprecipitated luminescent complex (AuCl)2L (L is cyclic PNNP ligand). Analysis of the data obtained by DLS, CD spectroscopy, luminescence derived from both (AuCl)2L and YFP reveal the electrostatically driven interaction of negatively charged proteins with the shell of PEI-(AuCl)2L. The fluorescence of YFP enables to reveal the inclusion of the protein molecules into the shell. The lack of any luminescent response of PEI-(AuCl)2L on TRX conforms its electrostatically driven interactions with the shell which, in turn, excludes a binding of the exposed thiol moieties with (AuCl)2L. The negatively charged surface of pepsin provides the greatest recharging of the PEI-based shell versus the other proteins, which is followed by the enhanced luminescence of (AuCl)2L. The significant effect of PEI-(AuCl)2L on the CD spectra of LSZ followed by the decreased intensity of (AuCl)2L-based luminescence points to specific interaction mode of PEI-(AuCl)2L with LSZ. The flow cytometry and fluorescent microscopy measurements revealed efficient internalization of PEI-(AuCl)2L into the Wi-38 cell samples resulting in the efficient staining of all cell organelles. The concentration dependent cytotoxicity of PEI-(AuCl)2L is detectably enhanced by LSZ, which is correlated with its interaction mode with the nanoparticles.



中文翻译:

带相反电荷的壳和核对核-壳胶体与带不同电荷的蛋白质相互作用的影响,作为调节胶体细胞毒性的途径。

本工作代表了核-壳纳米颗粒与不同蛋白质之间的相互作用,例如溶菌酶(LSZ),胃蛋白酶,牛血清白蛋白(BSA),硫氧还蛋白(TRX)和黄色荧光蛋白(YFP)。核-壳形态源自聚乙烯亚胺(PEI)在纳米沉淀发光复合物(AuCl)2 L(L为环状PNNP配体)上的非共价沉积。对通过DLS,CD光谱,(AuCl)2 L和YFP两者获得的发光进行的数据分析表明,带负电的蛋白质与PEI-(AuCl)2 L的壳之间存在静电相互作用。YFP的荧光能够揭示蛋白质分子进入外壳。PEI-(AuCl)没有任何发光响应TRX上的2 L符合其与壳的静电驱动相互作用,从而排除了暴露的硫醇部分与(AuCl)2 L的结合。胃蛋白酶带负电荷的表面为基于PEI的壳提供了最大的充电(AuCl)2 L的增强发光。PEI-(AuCl)2 L对LSZ CD光谱的显著作用,其后基于(AuCl)2 L的发光强度降低,指向PEI-(AuCl)2 L与LSZ的特定相互作用模式 流式细胞仪和荧光显微镜测量显示PEI-(AuCl)2的有效内在化L进入Wi-38细胞样品,导致所有细胞器的有效染色。LSZ可检测到PEI-(AuCl)2 L的浓度依赖性细胞毒性,这与其与其与纳米颗粒的相互作用方式有关。

更新日期:2020-08-15
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