Alzheimer's and Dementia: New antibodies target tau protein oligomers and promote the removal of lysosomes of tau proteins in cells

Tau is a neuron micro-tube-related protein that aggregates insoluble fibrous deposits in a series of neurodegenerative diseases called tau diseases.
Alzheimer's disease (AD) is characterized by the presence of extracellular plaques and in-cell tau tangles consisting of amyloid protein β (A beta).
have tried several treatments for A-beta pathology, but so far they have failed to show significant benefits in clinical trials.
, treatments for tau pathology have become very important, especially since AD's cognitive decline is better associated with tau pathology than with amyloid burden.
previous studies have found several treatments based on small molecules aimed at reducing tau aggregation, which seems promising in animal models but has failed in clinical trials, so tau-based immunotherapy may be more promising.
recently, researchers published a paper in the journal Alzheimer's and Dementia reporting on the development of monoclonal antibodies for purified low n tau repetitive domain lymers as a tool to mediate tau aggregation and toxicity.
researchers tested in-body aggregation inhibition with sulfonin S, dynamic light scattering (DLS) and atomic force microscopy (AFM), and analyzed the inhibition of antibodies to aggregation in the N2a cell model of tau disease using a split luciferase complementary test and fluorescence-activated cell sephora (FACS).
results showed that the antibody inhibited tau aggregation in in-body by blocking tau's aggregation in a oligopoly state by about 90%.
test by dividing luciferase supplements, some antibodies were able to block tau's cojubination/multi-polymerization in cells.
applied outside the cell are internalized and cause tau to be sealed into lysosomes for degradation.
, novel low N-tau oligopolymer-specific monoclonal antibodies inhibit Tau oligomerization in cells and promote the removal of toxic tau.