Effect of tert-alcohol functional imidazolium salts on oligomerization and fibrillization of amyloid β (1–42) peptide

Abstract Imidazolium based IL's has gained vast interest in developing biological applications. Oligomerization and fibrillization of amyloid β (1–42) peptide are mainly responsible for the extra-neuronal deposition of amyloid fibrils in neurodegenerative disorders like Alzheimer's disease (AD). Here, we report an effect of tert-BuOH-functional imidazolium ILs on oligomerization and fibrillization of amyloid β (1–42) Peptide in vitro. In this study, a series of these [alkyl-tOHim][OMs] ILs with methyl sulphonate counter anion by varying alkyl chains were used. Among the seven protic ILs, four showed strong binding and inhibition activity for the formation of amyloid β (1–42) aggregation by using Thioflavin T fluorescence binding assay. The secondary structural analysis of the peptide, pre-incubated with active ILs shows the loss of ordered β-sheet amyloid structure. The longer alkyl chain ILs showed that an increased in amyloid binding and hence an inhibition effect on amyloid aggregation was enhanced. Thus, we propose that ILs could be presented as potential candidates for therapeutic intervention against Alzheimer's disease (AD).