On the role of methanol in amyloid formation induction in apo-yeast alcoholdehydrogenase

Amyloid formation in non disease proteins has little been studied. In the present study, to reveal the trend of amyloid formation in a typical protein, apo I- yeast alcohol dehydrogenase (apo I-YADH) which was obtained by removing of the structural zinc, was subjected to aqueous solution of methanol. Amyloid formation was evaluated by Congo red (CR) and thioflavin T staining method using fluorescence and CD spectroscopy. The amyloid-inducing aptitude of methanol showed a concentration dependent manner: 20% 40%  60% 70% 80%. The established amyloid formation monitored by spectroscopic studies, was ascribed to the conformational transition from native to the ß-sheet rich structure in the enzyme molecules.