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

TitleEffect of tert-alcohol functional imidazolium salts on oligomerization and fibrillization of amyloid beta (1-42) peptide
Publication TypeJournal Article
Year of Publication2020
AuthorsSaid, MS, Navale, GR, Yadav, A, Khonde, N, Shinde, SS, Jha, A
JournalBiophysical Chemistry
Volume267
Pagination106480
Date PublishedDEC
Type of ArticleArticle
ISSN0301-4622
KeywordsAggregation, Amyloid beta (1-42) peptide, Biofilm inhibitor, Imidazolium ionic liquid
Abstract

Imidazolium based IL's has gained vast interest in developing biological applications. Oligomerization and fibrillization of amyloid beta (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 beta (1-42) Peptide in vitro. In this study, a series of these [alkyl-(t)OHim][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 beta (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 beta-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).

DOI10.1016/j.bpc.2020.106480
Type of Journal (Indian or Foreign)

Foreign

Impact Factor (IF)

1.995

Divison category: 
Organic Chemistry

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