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Dual function of Selenium nanoparticles: Inhibition or induction of lysozyme amyloid aggregation and evaluation of their cell based cytotoxicity.
Archives Italiennes De Biologie ( IF 1 ) Pub Date : 2021-6-30 , DOI: 10.12871/00039829202123
H Ramshini 1 , S Rostami
Affiliation  

Aberrant protein aggregation and the formation of amyloid deposits are associated with numerous neuro- and non-neurodegenerative disorders. Thus, one potential strategy is to eliminate these deposits by halting amyloid aggregation. Selenium nanoparticles (Se-NPs) have great potential in biomedicine for various therapeutic and diagnostic purposes and also have the ability to inhibit amyloid fibrillation. Herein, Hen Egg White Lysozyme (HEWL) was chosen as a protein model, and rod-like Se-NPs with diameters ranging from 90 to 120 nm were synthesized and the influence of shape and concentration of the particles on HEWL fibrillation was investigated. The effect of the nanoparticles on HEWL amyloid formation was analyzed using thioflavin T and Congo red binding assays, atomic force microscopy, and cytotoxicity assays. In the present study, it has been observed that these particles have a dual function in various concentrations. Using lower concentrations of Se-NPs ranging from 3-30 μg/ml, the Thioflavin T (ThT) fluorescence intensity decreased significantly by 60%, with an increased lag time compared to that of the control. While HEWL fibrillation substantially increased upon co-incubation with a higher concentration of these particles (300-2400μg/ml), and these results were verified by AFM, Congo red, and MTT assay. We showed that inhibitory or inductive influences of Se-NPs on the hen egg-white lysozyme (HEWL) amyloid aggregation are achieved via different independent mechanisms. These results demonstrate that dual-activity of Se-NPs might be a valuable targeting system for inhibiting amyloid aggregation, and thus, may play a useful role in new therapeutic and diagnostic strategies for amyloid-related disorders.

中文翻译:

硒纳米颗粒的双重功能:抑制或诱导溶菌酶淀粉样蛋白聚集并评估其基于细胞的细胞毒性。

异常的蛋白质聚集和淀粉样沉积物的形成与许多神经和非神经退行性疾病有关。因此,一种潜在的策略是通过停止淀粉样蛋白聚集来消除这些沉积物。硒纳米颗粒 (Se-NPs) 在生物医学中具有巨大的潜力,可用于各种治疗和诊断目的,并且还具有抑制淀粉样蛋白纤维化的能力。在本文中,选择鸡蛋清溶菌酶(HEWL)作为蛋白质模型,合成直径为 90 至 120 nm 的棒状硒纳米颗粒,并研究了颗粒形状和浓度对 HEWL 纤维化的影响。使用硫代黄素 T 和刚果红结合测定、原子力显微镜和细胞毒性测定分析纳米颗粒对 HEWL 淀粉样蛋白形成的影响。在目前的研究中,已经观察到这些粒子在不同浓度下具有双重功能。使用 3-30 μg/ml 范围内的较低浓度的 Se-NP,硫黄素 T (ThT) 荧光强度显着降低了 60%,与对照相比,滞后时间增加。而 HEWL 原纤维在与更高浓度的这些颗粒 (300-2400μg/ml) 共同孵育后显着增加,并且这些结果已通过 AFM、刚果红和 MTT 测定验证。我们表明,Se-NPs 对鸡蛋清溶菌酶 (HEWL) 淀粉样蛋白聚集的抑制或诱导影响是通过不同的独立机制实现的。这些结果表明,Se-NPs 的双重活性可能是抑制淀粉样蛋白聚集的有价值的靶向系统,因此,
更新日期:2021-07-01
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