New Approaches Detection Secondary Conformation of Prion Protein in Frozen-Section Tissue by Fourier-Transform Infrared Microscopy

摘要

The spectra and the relative ratio of the secondary conformations (a-helix and (3-sheet) of prion infected brains in frozen sectioned tissue were measured by Fourier-transform infrared (FT-IR) microscopy. The tissues were obtained from the Prion Diseases Research Center in the National Animal Health Institute (PDRC/NAHI) of Japan. Both prion infected and normal brain tissues of mice and hamster were embedded adjacently and were frozen-sectioned for the FT-IR microscopy. Spectra from the normal and the prion-infected brain tissue sides were compared, The C-H stretching components in the normal tissue and the amide-I, -II components in the prion tissue were larger than the other sides, respectively. Furthermore, we developed the software to analyze the relative ratios of protein secondary conformation in the tissue by FT-IR microscopy.