Irradiation effect of a submillimeter wave from 420 GHz gyrotron on amyloid peptides in vitro

Takayasu Kawasaki; Yuusuke Yamaguchi; Tomomi Ueda; Yuya Ishikawa; Toyonari Yaji; Toshiaki Ohta; Koichi Tsukiyama; Toshitaka Idehara; Masatoshi Saiki; Masahiko Tani

doi:10.1364/BOE.395218

Irradiation effect of a submillimeter wave from 420 GHz gyrotron on amyloid peptides in vitro

Biomed Opt Express. 2020 Aug 31;11(9):5341-5351. doi: 10.1364/BOE.395218. eCollection 2020 Sep 1.

Authors

Affiliations

¹ 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.
² Research Center for Development of Far-Infrared Region, University of Fukui, 3-9-1 Bunkyo, Fukui, Fukui 910-8507, Japan.
³ Department of Applied Chemistry, Faculty of Engineering, Sanyo-Onoda City University, 1-1-1 Daigakudori, Sanyo-Onoda, Yamaguchi 756-0884, Japan.
⁴ SR Center, Research Organization of Science and Technology, Ritsumeikan University, 1-1-1 Noji-Higasi, Kusatsu, Shiga 525-8577, Japan.

Abstract

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.