Redox behaviors of the neurotoxic portion in human prion protein, HuPrP(106-126)

► HuPrP(109-111) covers the copper-binding site around His111 in HuPrP(106-126). ► Redox activities of Cu-HuPrP(109-111) complexes depend on copper-binding conformations. ► N−-rich coordinations show high Cu(II)/Cu(III) oxidation activities. ► Methionine-interacted models have high Cu(II)/Cu(I) reduction activities. ► Such diverse redox behaviors could be involved in the neurotoxic mechanism of HuPrP(106-126).