Tunable inhibition of β-amyloid peptides by fast green molecules

The aggregation of β-amyloid (Aβ) protein into toxic intermediates and mature fibrils is considered to be one of the main causes of Alzheimer's disease (AD). Small molecules as one of blockers are expected to be the potential drug treatment for the disease. However, the nucleation process in molecular assembly is less informative in the literatures. In this work, the formation of Aβ (16-22) peptides was investigated with the presence of small molecule of fast green (FG) at the initial aggregation stage. The results exhibited the tunable inhibitory ability of FG molecules on Aβ (16-22) peptides. Atomic force microscopy (AFM) demonstrated that the inhibitory effect would be dependent on the dose of FG molecules, which could delay the lag time (nucleation) and form single layer conjugates. Spectral measurements further showed that the β-sheet secondary structure of Aβ (16-22) reduced dramatically after the presence of FG molecules. Instead, non-β-sheet nanosheets were formed when the FG/Aβ (16-22) ratio reached 1:1. In addition, the cytotoxicity of aggregates reduced greatly with the presence of FG molecules compared with the Aβ (16-22) fibrils. Overall, this study provided a method for suppressing the toxic amyloid aggregates by FG molecules efficiently, and also showed a strategy for fabrication of two-dimensional materials by small molecules.     

多个布儒斯特窗大型光学元件的损伤在线检测

 针对高功率固体激光装置主放大器中以布儒斯特角放置的大型光学元件，设计了一套损伤在线检测系统。该系统利用望远系统倍率不变特性实现了多个光学元件在线等精度、等分辨率检测；采用景深理论，通过仔细调节孔径光阑的大小，以达到既能测量同一倾斜光学元件上的不同损伤点，又能减小相邻光学元件间损伤信息相互影响的目的。通过亮场成像纵向定位损伤位置，而利用暗场成像横向定位损伤的大小。实验证明了该方法的可行性和有效性。该检测方法适用于各种多个倾斜放置的光学元件的损伤在线检测。