EGCG impedes human Tau aggregation and interacts with Tau

Area of Science:

• Neuroscience
• Biochemistry
• Pharmacology

Background:

• Tau aggregation is central to Alzheimer's disease (AD) pathogenesis.
• Inhibiting Tau aggregation is a promising therapeutic strategy for AD.
• Phytochemicals, like EGCG from green tea, are explored for their anti-aggregation properties.

Purpose of the Study:

• To investigate the effect of Epigallocatechin-3-gallate (EGCG) on the aggregation and disassembly of full-length human Tau.
• To determine the binding affinity of EGCG to Tau.
• To explore EGCG as a potential therapeutic agent for Alzheimer's disease.

Main Methods:

• Thioflavin S (ThS) fluorescence assay
• MALDI-TOF analysis
• Isothermal Titration Calorimetry (ITC)

Main Results:

• EGCG demonstrated a dual effect, inhibiting Tau aggregation and promoting the disassembly of existing Tau aggregates.
• The IC50 for EGCG's inhibition of Tau aggregation was determined to be 64.2 μM.
• Binding affinity studies quantified the interaction between EGCG and Tau.

Conclusions:

• EGCG exhibits significant potential as a therapeutic agent for Alzheimer's disease by modulating Tau aggregation.
• The dual action of EGCG on Tau aggregation and disassembly warrants further investigation for drug development.
• EGCG's interaction with Tau provides a molecular basis for its neuroprotective effects in Alzheimer's disease.