Abstract
The contribution of the dynamic water structure to amyloid formation in yeast alcohol dehydrogenase (YADH) was studied in an aqueous solution of alcohol. The water structure is determined by the alcohol concentration dependence of the spin-lattice relaxation time of a water molecule in pure alcohol/water. The structure of YADH was found to depend on its environment in aqueous media and to form the amyloid with four alcohols (methanol, ethanol, iso-propanol and tert-butanol) after conformational transition to a β-sheet-rich structure determined by circular dichroism spectroscopy and Congo red or Thioflavine T staining. The alcohol concentration required to induce the amyloid formation decreased with the increasing carbon number (hydrophobicity) in the alcohols. The dynamic water structure in an aqueous solution of alcohol also increases with the increasing carbon number in the alcohols and was found to correlate well with the midpoint concentration of the alcohol for forming the amyloid of YADH in an aqueous solution of alcohol. Therefore, we concluded that the amyloid formation of YADH in an aqueous solution of alcohol was promoted by the strong attraction of water molecules toward the alcohol molecules (dehydration).
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