Kawasaki Takayasu, Yamaguchi Yuusuke, Ueda Tomomi, Ishikawa Yuya, Yaji Toyonari, Ohta Toshiaki, Tsukiyama Koichi, Idehara Toshitaka, Saiki Masatoshi, Tani Masahiko
IR-FEL Research Center, Research Institute for Science and Technology, Organization for Research Advancement, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan.
Research Center for Development of Far-Infrared Region, University of Fukui, 3-9-1 Bunkyo, Fukui, Fukui 910-8507, Japan.
Biomed Opt Express. 2020 Aug 31;11(9):5341-5351. doi: 10.1364/BOE.395218. eCollection 2020 Sep 1.
On using the far-infrared radiation system, whether the irradiation effect is thermal or non-thermal is controversial. We irradiated amyloid peptides that are causal factors for amyloidosis by using a submillimeter wave from 420 GHz gyrotron. Fluorescence reagent assay, optical and electron microscopies, and synchrotron-radiation infrared microscopy showed that the irradiation increased the fibrous conformation of peptides at room temperature for 30 min. The temperature increase on the sample was only below 5 K, and a simple heating up to 318 K hardly induced the fibril formation. Therefore, the amyloid aggregation was driven by the far-infrared radiation with little thermal effect.
在使用远红外辐射系统时，其照射效果是热效应还是非热效应存在争议。我们使用420吉赫兹回旋管产生的亚毫米波照射作为淀粉样变性病因的淀粉样肽。荧光试剂检测、光学和电子显微镜以及同步辐射红外显微镜显示，在室温下照射30分钟会增加肽的纤维构象。样品温度仅升高不到5K，简单加热到318K几乎不会诱导原纤维形成。因此，淀粉样聚集是由几乎没有热效应的远红外辐射驱动的。
