Exploration of Insulin Amyloid Polymorphism Using Raman Spectroscopy and Imaging.

ABSTRACT: We aimed to investigate insulin amyloid fibril polymorphism caused by salt effects and heating temperature and to visualize the structural differences of the polymorphisms in situ using Raman imaging without labeling. The time course monitoring for amyloid formation was carried out in an acidic condition without any salts and with two species of salts (NaCl and Na₂SO₄) by heating at 60, 70, 80, and 90°C. The intensity ratio of two Raman bands at 1672 and 1657 cm^-1 due to antiparallel β-sheet and α-helix structures, respectively, was revealed to be an indicator of amyloid fibril formation, and the relative proportion of the β-sheet structure was higher in the case with salts, especially at a higher temperature with Na₂SO₄. In conjunctio

SUBMITTER: Ishigaki M 

PROVIDER: S-EPMC7300310 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature