Jiang Zhiqiang, Dong Xiaoyan, Sun Yan
Department of Biochemical Engineering and Key Laboratory of Systems Bioengineering (Ministry of Education), School of Chemical Engineering and Technology, Tianjin University, Tianjin 300354, China.
Department of Biochemical Engineering and Key Laboratory of Systems Bioengineering (Ministry of Education), School of Chemical Engineering and Technology, Tianjin University, Tianjin 300354, China.
Carbohydr Res. 2018 May 22;461:11-18. doi: 10.1016/j.carres.2018.03.001. Epub 2018 Mar 8.
Amyloid β-protein (Aβ) aggregation is crucial for the pathogenesis of Alzheimer's disease, and surface charge of nanoparticles (NPs) has been recognized as an important factor influencing Aβ aggregation. Herein, we report a systematic study on the issue with a series of self-assembled chitosan-hyaluronic acid composite (CH) NPs of different surface charges (CH1 to CH7, zeta potentials from +38 to -35 mV). Both the positive and negative CH NPs inhibited Aβ aggregation and the inhibitory effect increased with increasing the surface charges density. Circular dichroism spectroscopy and atomic force microscopy revealed the difference in their working mechanisms. Studies at different pH values further confirmed the importance of electrostatic interactions in Aβ aggregation and presented that the effects of CH NPs changed due to the change of Aβ charge property with pH. This work has thus provided new insight into the surface charge effects on Aβ aggregation.
淀粉样β蛋白(Aβ)聚集对阿尔茨海默病的发病机制至关重要,纳米颗粒(NPs)的表面电荷已被认为是影响Aβ聚集的一个重要因素。在此,我们报道了对该问题的一项系统性研究,该研究使用了一系列具有不同表面电荷(CH1至CH7,ζ电位从+38至-35 mV)的自组装壳聚糖-透明质酸复合(CH)纳米颗粒。带正电和带负电的CH纳米颗粒均抑制Aβ聚集,且抑制作用随表面电荷密度的增加而增强。圆二色光谱和原子力显微镜揭示了它们作用机制的差异。在不同pH值下的研究进一步证实了静电相互作用在Aβ聚集中的重要性,并表明由于Aβ电荷性质随pH值变化,CH纳米颗粒的作用也发生了改变。因此,这项工作为表面电荷对Aβ聚集的影响提供了新的见解。