Interaction of a new copper(II) complex with PrP: effects on protein aggregation

In this work, we evaluated the potential of the copper(II) complex CuIPMFF as a modulator of prion protein (PrP) aggregation, a key process in the progression of prion diseases. The complex contains a tripodal ligand with three different rings: a piridine, a methylimidazole and a phenol. Coordination sphere is completed by two chlorido ligands. Circular dichroism has shown that complex preserves the native conformation of monomeric PrP, while thioflavin T assays demonstrated a significant reduction and delay of protein aggregation in a concentration-dependent manner. These findings highlight CuIPMFF as a promising lead compound for the development of therapeutic strategies targeting PrP misfolding and aggregation.