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搅拌湿磨对 AsS 纳米颗粒与白蛋白之间纳米-生物界面的影响。

Nano-bio interface between AsS nanoparticles and albumin influenced by wet stirred media milling.

机构信息

Institute of Geotechnics, Slovak Academy of Sciences, Watsonova 45, 04001 Košice, Slovakia.

Institute of Geotechnics, Slovak Academy of Sciences, Watsonova 45, 04001 Košice, Slovakia.

出版信息

Int J Pharm. 2023 Jun 10;640:123046. doi: 10.1016/j.ijpharm.2023.123046. Epub 2023 May 12.

DOI:10.1016/j.ijpharm.2023.123046
PMID:37178791
Abstract

Arsenic sulfide (AsS) nanoparticles have been intensively researched as a promising drug in a cancer treatment. For the first time, the interaction between AsS and bovine serum albumin has been studied in this paper. Initially, the sorption kinetics of albumin on the surface of nanoparticles was investigated. Subsequently, its structural changes influenced by interaction with the AsS nanoparticles during wet stirred media milling were studied in deep. Both the dynamic and static quenching were detected after analyzing the fluorescence quenching spectra. From the synchronous fluorescence spectra it was investigated, that the fluorescence intensity for tyrosine residues decreased by about 55%, and for tryptophan it was about 80%. It indicates the fluorescence from tryptophan is more intense and gets more efficiently quenched than those from tyrosine residues in presence of AsS, implying that the tryptophan can be closer to the binding site. From the circular dichroisms and FTIR spectra it was observed that conformation of the protein remains almost unchanged. The content of appropriate secondary structures was determined by deconvolution of the absorption peak attributed to the amide I band in FTIR spectra. The preliminary anti-tumor cytotoxic effect of prepared albumin-AsS system was also tested on multiple myeloma cell lines.

摘要

硫化砷(AsS)纳米粒子已被广泛研究作为癌症治疗中的一种有前途的药物。本文首次研究了 AsS 与牛血清白蛋白之间的相互作用。首先,研究了白蛋白在纳米粒子表面的吸附动力学。随后,深入研究了在湿搅拌介质研磨过程中与 AsS 纳米粒子相互作用时其结构变化。通过分析荧光猝灭光谱,检测到了动态和静态猝灭。从同步荧光光谱可以看出,色氨酸残基的荧光强度降低了约 55%,而色氨酸的荧光强度降低了约 80%。这表明在存在 AsS 的情况下,色氨酸的荧光强度更强,并且更有效地猝灭,这意味着色氨酸可以更接近结合位点。从圆二色性和傅里叶变换红外光谱可以观察到,蛋白质的构象几乎保持不变。通过对傅里叶变换红外光谱中酰胺 I 带归因于吸收峰的解卷积,确定了适当的二级结构含量。还在多发性骨髓瘤细胞系上测试了制备的白蛋白-AsS 系统的初步抗肿瘤细胞毒性作用。

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Nanomaterials (Basel). 2020 Dec 30;11(1):69. doi: 10.3390/nano11010069.