Protein Misfolding Modulators

Aldose Reductase Inhibitor can Inhibit tau Aggregation.

 

Alzheimer's disease is often referred as protein misfolding disease through peptide plaque accumulation of abnormally folded amyloid such as beta amyloid (Aβ) and tau amyloid protein in the brain system. According to the precedent reviews, some aggregation inhibitors of tau protein as well as selected amyloids are becoming a cornerstone of the capable chemotherapy for Alzheimer disease and other neurodegenerative symptoms.

 

 

 

Among the emerging small molecule tau inhibitors, particular heterocyclic structural motifs such as rhodanines and cyanine dyes are highlighted as promising and privileged key pharmacophores. Guided by these precedent findings, we are interested in the behavior and inhibitory functions of some generic (classical) drugs with traditional pigment skeletons towards tau protein aggregation. Thus, described herein is our preliminary investigation on the modulating activity of the aldose reductase inhibitor eparlestat on the tau aggregation under the in vitro experiments.

 

 

 

Rhodanine derivatives are classical heterocyclic dye materials, which recently have been investigated intensively by the German researchers towards tau interactions. Their previous results as well as commentary summary indicated the similar potency of the generic drug eparlestat, in view of the pre-existing nontoxic drugs, although no experimental results available. Thus, in order to gain a precise knowledge and evaluate the exact pleiotropic effects of eparlestat on tau aggregation, we have been investigating of some existing generic drugs along these lines, as summarized below.

 

In our preliminary in vitro experiments, three generic drugs at hands are investigated towards tau aggregation inhibitory activity along with the known methylene blue as a positive standard.