Nov 13, 2019

Melatonin interacts with repeat domain of Tau to mediate disaggregation of paired helical filaments

Biochimica Et Biophysica Acta. General Subjects
Abhishek Ankur BalmikSubashchandrabose Chinnathambi

Abstract

Tau is the major neuronal protein involved in the stabilization of microtubule assembly. In Alzheimer's disease, Tau self-assembles to form intracellular protein aggregates which are toxic to cells. Various methods have been tried and tested to restrain the aggregation of Tau. Most of the agents tested for this purpose have limitations in their effectiveness and availability to neuronal cells. We have tested melatonin, a neurohormone secreted by pineal gland and a well-known anti-oxidant, for its ability to interact with the repeat domain of Tau using ITC and NMR. In aggregation inhibition and disaggregation studies of repeat Tau, melatonin was found to modulate the aggregation propensity of repeat Tau at a concentration of 5000 μM and was more effective in dissolving preformed aggregates rather than acting as an aggregation inhibitor. However, there were no major conformational changes in Tau in presence of melatonin as observed by CD spectroscopy. On the basis of our findings, we are proposing a mechanism by which melatonin can interact with the repeat domain of Tau and exhibit its disaggregation effect.

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Mentioned in this Paper

Study
Neurons
Antioxidants
Melatonin
Alzheimer's Disease
Pharmacologic Substance
Protein Aggregation, Pathological
Tau Proteins
Microtubule-Associated Protein Tau
Neurohormones

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