Alzheimer's disease (AD) is a neurodegenerative disorder characterized by the accumulation of amyloid β (Aβ) plaques and neurofibrillary tangles (NFTs). Ferroptosis, an iron-dependent form of cell death, plays a significant role in AD pathogenesis through the generation of reactive oxygen species (ROS), mitochondrial damage, lipid peroxidation, and reduced glutathione peroxidase 4 (GPX4) enzyme activity. Liquid-liquid phase separation (LLPS) of tau drives the growth and maturation of NFTs, contributing to AD pathology. This study combines the structural and functional properties of gallic acid (GA) and cyclic dipeptides (CDPs) to synthesize hybrid molecules that target both ferroptosis and amyloid toxicity in AD. The innovative approach involves the first synthetic small molecule (GCTR) that effectively combats ferroptosis, restores GPX4 activity, and enhances GPX4 levels. GCTR also disrupts Fe³⁺-induced LLPS of tau and reduces abnormal tau fibrillation. The synergistic action of GCTR in combating ferroptosis and amyloid toxicity, along with its ability to enhance GPX4 and modulate Fe³⁺-induced tau LLPS, holds promise for the development of novel therapeutics for AD.Alzheimer's disease (AD) is a neurodegenerative disorder characterized by the accumulation of amyloid β (Aβ) plaques and neurofibrillary tangles (NFTs). Ferroptosis, an iron-dependent form of cell death, plays a significant role in AD pathogenesis through the generation of reactive oxygen species (ROS), mitochondrial damage, lipid peroxidation, and reduced glutathione peroxidase 4 (GPX4) enzyme activity. Liquid-liquid phase separation (LLPS) of tau drives the growth and maturation of NFTs, contributing to AD pathology. This study combines the structural and functional properties of gallic acid (GA) and cyclic dipeptides (CDPs) to synthesize hybrid molecules that target both ferroptosis and amyloid toxicity in AD. The innovative approach involves the first synthetic small molecule (GCTR) that effectively combats ferroptosis, restores GPX4 activity, and enhances GPX4 levels. GCTR also disrupts Fe³⁺-induced LLPS of tau and reduces abnormal tau fibrillation. The synergistic action of GCTR in combating ferroptosis and amyloid toxicity, along with its ability to enhance GPX4 and modulate Fe³⁺-induced tau LLPS, holds promise for the development of novel therapeutics for AD.