Peng Jian, Weng Jian, Ren Lei, Sun Li-Ping
Department of Biomaterials, College of Materials, Xiamen University, Xiamen 361005, People's Republic of China.
IET Nanobiotechnol. 2014 Dec;8(4):295-303. doi: 10.1049/iet-nbt.2013.0071.
Amyloid β25-35 (Aβ25-35) peptide is a peculiar peptide for its rapid aggregation properties and high neurotoxicity in Alzheimer's disease. Here, the interactions between gold nanoparticles (GNPs) and Aβ25-35 monomers, oligomers and fibrils are explored under different molar ratio, temperature and pH by ultraviolet-visible and circular dichroism spectra, thioflavin T fluorescence assay and transmission electron microscope. It is concluded that Aβ25-35 can induce the aggregation of GNPs at certain concentration of Aβ25-35 monomer or oligomer. But at higher concentration of Aβ25-35, GNPs aggregates dissociate again. Furthermore, the aggregation rate increases at higher temperature or for lower pH. These results might provide the basis of a simple diagnostic tool for detecting Alzheimer's disease.
淀粉样β蛋白25-35（Aβ25-35）肽因其在阿尔茨海默病中具有快速聚集特性和高神经毒性而成为一种特殊的肽。在此，通过紫外可见光谱和圆二色光谱、硫黄素T荧光测定法以及透射电子显微镜，在不同摩尔比、温度和pH条件下探究了金纳米颗粒（GNP）与Aβ25-35单体、寡聚体和原纤维之间的相互作用。得出的结论是，在一定浓度的Aβ25-35单体或寡聚体条件下，Aβ25-35可诱导GNP聚集。但在更高浓度的Aβ25-35时，GNP聚集体会再次解离。此外，在较高温度或较低pH条件下聚集速率会增加。这些结果可能为检测阿尔茨海默病的简单诊断工具提供依据。
