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

Autor: Said MS; Organic Chemistry Division, CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road, Pune 411008, India., Navale GR; Organic Chemistry Division, CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road, Pune 411008, India., Yadav A; Organic Chemistry Division, CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road, Pune 411008, India., Khonde N; Organic Chemistry Division, CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road, Pune 411008, India., Shinde SS; Organic Chemistry Division, CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road, Pune 411008, India. Electronic address: shinde88@gmail.com., Jha A; Nanobioscience Group, Agharkar Research Institute, G. G. Agarkar Road, Pune 411004, India. Electronic address: anjalijha@aripune.org.
Jazyk: angličtina
Zdroj: Biophysical chemistry [Biophys Chem] 2020 Dec; Vol. 267, pp. 106480. Date of Electronic Publication: 2020 Sep 21.
DOI: 10.1016/j.bpc.2020.106480
Abstrakt: 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- 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 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).
(Copyright © 2020. Published by Elsevier B.V.)
Databáze: MEDLINE
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