Researchers with Case Western Reserve University looked at the brain samples of 40 participants who suffered from Alzheimer’s disease (AD) upon becoming deceased.
Published in Science Translational Medicine, their recent study determined that the cores of tau protein particles have distinct structural organizations.
According to researchers, a link was found between strains of misshapen tau protein and accelerated cognitive decline. The new findings may lead to more precise diagnoses and interventions for patients with Alzheimer’s.
“Using sensitive biophysical methods in 40 patients with AD and markedly different disease durations, we identified populations of distinct TAU particles that differed in size, structural organization, and replication rate in vitro and in cell assay,” the authors explained in their findings.
“The rapidly replicating, distinctly misfolded TAU conformers found in rapidly progressive AD were composed of ~80% misfolded four-repeat (4R) TAU and ~20% of misfolded 3R TAU isoform with the same conformational signatures,” the authors also determined.
“These biophysical observations suggest that distinctly misfolded population of 4R TAU conformers drive the rapid decline in AD and imply that effective therapeutic strategies might need to consider not a singular species but a cloud of differently misfolded TAU conformers.”