Alzheimer's disease (AD) is a neurodegenerative disorder characterized by the accumulation of amyloid β-protein (Aβ) and tau protein in the brain. Aβ is derived from the β-amyloid precursor protein (APP) through sequential cleavage by β- and γ-secretase. Tau, a microtubule-associated protein, forms neurofibrillary tangles when hyperphosphorylated. These pathological features are central to AD pathogenesis and have been linked to both familial and sporadic forms of the disease. Genetic factors, such as mutations in the APP, presenilin 1 (PS1), and presenilin 2 (PS2) genes, contribute to the development of AD. The ε4 allele of apolipoprotein E (ApoE) is a known risk factor for AD. Recent advances in understanding the molecular mechanisms of AD have led to the development of therapeutic strategies targeting Aβ and tau. These include inhibitors of Aβ production, anti-aggregating agents, and immunotherapies. Active and passive immunotherapy have shown promise in reducing Aβ plaques and soluble Aβ levels in animal models. However, clinical trials have faced challenges, including side effects and variable efficacy. Mouse models of AD have been instrumental in studying the disease's progression and testing potential therapies. These models recapitulate key pathological features of AD, including Aβ plaques and neurofibrillary tangles. Studies have shown that soluble Aβ oligomers, rather than fibrils, may be the primary toxic species in AD. Targeting these oligomers is a promising therapeutic approach. Despite significant progress, many questions remain about the pathogenesis and treatment of AD. Ongoing research aims to develop more effective therapies that can prevent or slow the progression of the disease. Future approaches may include personalized risk assessments based on genetic and biomarker data, enabling early intervention for at-risk individuals.Alzheimer's disease (AD) is a neurodegenerative disorder characterized by the accumulation of amyloid β-protein (Aβ) and tau protein in the brain. Aβ is derived from the β-amyloid precursor protein (APP) through sequential cleavage by β- and γ-secretase. Tau, a microtubule-associated protein, forms neurofibrillary tangles when hyperphosphorylated. These pathological features are central to AD pathogenesis and have been linked to both familial and sporadic forms of the disease. Genetic factors, such as mutations in the APP, presenilin 1 (PS1), and presenilin 2 (PS2) genes, contribute to the development of AD. The ε4 allele of apolipoprotein E (ApoE) is a known risk factor for AD. Recent advances in understanding the molecular mechanisms of AD have led to the development of therapeutic strategies targeting Aβ and tau. These include inhibitors of Aβ production, anti-aggregating agents, and immunotherapies. Active and passive immunotherapy have shown promise in reducing Aβ plaques and soluble Aβ levels in animal models. However, clinical trials have faced challenges, including side effects and variable efficacy. Mouse models of AD have been instrumental in studying the disease's progression and testing potential therapies. These models recapitulate key pathological features of AD, including Aβ plaques and neurofibrillary tangles. Studies have shown that soluble Aβ oligomers, rather than fibrils, may be the primary toxic species in AD. Targeting these oligomers is a promising therapeutic approach. Despite significant progress, many questions remain about the pathogenesis and treatment of AD. Ongoing research aims to develop more effective therapies that can prevent or slow the progression of the disease. Future approaches may include personalized risk assessments based on genetic and biomarker data, enabling early intervention for at-risk individuals.