This study presents a novel approach to combat Alzheimer's disease (AD) by developing hybrid molecules that synergistically target both ferroptosis and amyloid-associated toxicities. The hybrid molecules, synthesized from gallic acid (GA) and cyclic dipeptides (CDPs), effectively mitigate ferroptosis, a Fe-dependent form of cell death, and amyloid toxicity, which are key contributors to AD pathogenesis. The hybrid molecule GCTR was found to be particularly effective, as it not only chelates Fe³⁺ but also inhibits the aggregation of Aβ₄₂ and its complex with Fe³⁺, reduces reactive oxygen species (ROS) production, and prevents mitochondrial damage. GCTR also disrupts Fe³⁺-induced liquid-liquid phase separation (LLPS) of tau, which is a critical step in the formation of neurofibrillary tangles (NFTs) in AD. Additionally, GCTR restores the enzymatic activity of glutathione peroxidase 4 (GPX4), a key enzyme in the defense against ferroptosis, and enhances its cellular levels, further protecting cells from oxidative stress and neuronal death. The study demonstrates that GCTR is a promising small molecule-based therapeutic agent for AD, as it simultaneously targets both ferroptosis and amyloid toxicity, offering a new strategy for the treatment of this neurodegenerative disorder. The results highlight the potential of hybrid molecules in developing novel therapeutics for AD by combining the structural and functional properties of GA and CDPs.This study presents a novel approach to combat Alzheimer's disease (AD) by developing hybrid molecules that synergistically target both ferroptosis and amyloid-associated toxicities. The hybrid molecules, synthesized from gallic acid (GA) and cyclic dipeptides (CDPs), effectively mitigate ferroptosis, a Fe-dependent form of cell death, and amyloid toxicity, which are key contributors to AD pathogenesis. The hybrid molecule GCTR was found to be particularly effective, as it not only chelates Fe³⁺ but also inhibits the aggregation of Aβ₄₂ and its complex with Fe³⁺, reduces reactive oxygen species (ROS) production, and prevents mitochondrial damage. GCTR also disrupts Fe³⁺-induced liquid-liquid phase separation (LLPS) of tau, which is a critical step in the formation of neurofibrillary tangles (NFTs) in AD. Additionally, GCTR restores the enzymatic activity of glutathione peroxidase 4 (GPX4), a key enzyme in the defense against ferroptosis, and enhances its cellular levels, further protecting cells from oxidative stress and neuronal death. The study demonstrates that GCTR is a promising small molecule-based therapeutic agent for AD, as it simultaneously targets both ferroptosis and amyloid toxicity, offering a new strategy for the treatment of this neurodegenerative disorder. The results highlight the potential of hybrid molecules in developing novel therapeutics for AD by combining the structural and functional properties of GA and CDPs.