Abstract
We have investigated the effect of applying cryogenic temperature (–196℃) on three amyloid aggregates (human α-synuclein, bovine insulin, and hen egg lysozyme) using Fourier-transform infrared (FTIR) spectroscopy. The peak at ~1620 cm–1 indicating the intermolecular β-sheet structure of lysozyme amyloid structure increases after cooling, and those of the α-synuclein and insulin amyloid structures slightly decrease. These results mean that cryogenic temperature promoted the formation of lysozyme amyloid and led to a slight dissociation of α-synuclein and insulin amyloid. Our results indicate that the cryogenic temperature effect on the amyloid aggregates is small.
