Amyloid Peptide Self-Assembly in Protic Ionic Liquids

摘要

Amyloid proteins are renowned for their ability to self-assemble into highly ordered fibrils which are associated with diseases such as Parkinson disease, type II diabetes and Alzheimer's disease [1]. These fibrils are the result of a complex protein folding pathway that is still intensely debated among scientists worldwide. Currently, the neurotoxic species in the amyloid fibril assembling process is thought to be some form of soluble oligomer, most likely those that form from the early stages of Aβ aggregation [2,3]. Recent trends have been directed at finding ways to control amyloid self-assembly to allow for early state oligomer characterization [4]. New designer solvents such as protic ionic liquids (pILs) have received increased attention in protein refolding and renaturing studies [5,6]. Because the formation of amyloid fibrils proceeds via the formation of intramolecular hydrogen bonds, a selection of pILs with distinctly different hydrogen bonding abilities were investigated to better control the fibrilization process of Aβ_(16-22) These pILs consist of the common cation, triethylammonium (Tea), and various anions including dihydrogen phosphate (H2PO4), hydrogen sulfate (HSO4), trifiuoro acetate (Tfac), lactate (La), triflate (Tf) and mesylate (Ms).