Tau aggregation inhibiting peptides as a basis for future therapies for tauopathies
- Tau aggregation inhibiting peptides
- Strongly bind to tau monomers, -oligomers and -fibrils
- Suitable for future tauopathy therapies
A group of neurodegenerative disorders, including Alzheimer’s disease, Pick disease and Progressive supranuclear palsy are associated with neurofibrillary tangles composed of the tau protein as well as toxic tau oligomers. Therefore, inhibitors or modulators of tau-protein aggregation are being extensively investigated as potential new therapeutics. Two hexapeptides within tau, PHF6* (275VQIINK280) and PHF6 (306VQIVYK311), are known to be essential for tau aggregation, though PHF6* has recently been described as the stronger driver.
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The technology describes PHF6* fibril binding peptides consisting of D-enantiomeric amino acids. D-enantiomeric peptides are extremely protease-stable and considerably less immunogenic than L-peptides, and the suitability of D-peptides for in vivo applications has already been clearly demonstrated. The most interesting peptide, designated MMD3, was additionally found in a selection against tau monomer. MMD3 and its retro-inverso form, designated MMD3rev, clearly inhibits PHF6* and full length tau fibrilization in vitro.
- Tau aggregation inhibiting peptides for future tauopathy therapies
- Capable of binding to monomeric and aggregates of tau-protein, in particular tau-fibrils