Valence-sensitive assembly of a Cu-amyloid peptide network

External influences including biopolymers and transition metal ions have been shown to direct nucleation-driven peptide assembly from heterogenous configurations into homogeneous assemblies. A model congener of the Aβ peptide, HHQALVFFA-NH₂, reveals a valence-dependent templating effect in the presence of Cu(II) vs. Cu(I). Circular dichroism marks an increased aggregation rate with the Cu(I) template from >2 months to 90 min while still preserving the robust oxidizing properties engendered through the Cu-peptide lattice. Collectively, we demonstrate that a template ion's oxidation state can impact the growth kinetics of the cross-β network it seeds. These findings underscore how redox-state can transform inhibitory metal-peptide interactions into productive nucleation. Such control over assembly kinetics highlights an underexplored toggle for modulating amyloid growth.