Alzheimer's disease (AD) is the most common form of dementia and is the 6th leading cause of death in the United States. The current paradigm implicates the accumulation of amyloid-beta (Aβ) aggregates within the brain and cellular internalization as a factor for AD pathogenesis. A major cellular receptor for Aβ is the cellular prion protein (PrPC) which binds to Aβ in its N-terminal domain and central region according to in vitro assays. As the endocytosis of PrPC requires the coordination of metal ions, such as Cu2+, we propose that Aβ, PrPC, and Cu2+ form a ternary complex that is endocytosed as a unit leading to disease propagation and toxic interactions in neurons. A dilemma with studying the interaction between these two proteins is that the binding domains on each protein for each other, as well as Cu2+, are in intrinsically disordered regions, making it hard to study using single structure techniques. However, using a combinational approach with magnetic resonance techniques, a full picture of the ternary complex can be resolved. Previous and new 1H-15N heteronuclear single quantum coherence (HSQC) spectra show significant and unique chemical shift perturbations in residues on both proteins in the presence of each other with Cu2+. Furthermore, our recent electron spin-echo envelope modulation (ESEEM) EPR experiments show that nuclei from each protein coordinate to Cu2+, both supporting a ternary complex model. Future experiments in both these techniques, along with double electron-electron resonance (DEER) EPR will be used to continue exploring the ternary complex. Together, this research will improve our understanding of the interactions and endocytic pathway of Aβ with PrPC and Cu2+, paving the way for a new therapeutic approach in AD.