Nicolò Bisi

This paper designs a synthetic peptide mimicking Hsp90-Tau interaction to inhibit Tau aggregation and restore its microtubule binding, showing efficacy in vitro and in cells.

This paper uses peptidomimetic foldamers to study tau misfolding by inducing specific conformations of PHF6 and PHF6* sequences, showing that extended conformations drive aggregation while β-hairpins prevent it.

The paper uses live-cell imaging to identify a drug candidate that restores microtubule regulation by targeting tau aggregation and phosphorylation in a tauopathy model.