Amyloid beta (Aβ) is a peptide derived from the amyloid precursor protein (APP) through cleavage by β- and γ-secretases. Aβ accumulation in the brain is considered an early toxic event in Alzheimer's disease (AD), which is the most common form of dementia. The physiological and pathological forms of Aβ, as well as the mechanisms by which Aβ causes dementia, are not fully understood. Currently, there are no effective drugs to stop or reverse AD progression. This review discusses the structure, biological functions, and neurotoxicity of Aβ, potential receptors that interact with Aβ, and therapeutic strategies for AD. It also summarizes recent advances in Aβ-targeted therapies, including small molecules, vaccines, and antibodies against Aβ, as well as inhibitors of β- and γ-secretases, Aβ-degrading proteases, and tau protein inhibitors. The structure of Aβ is complex, with different conformations such as monomers, oligomers, protofibrils, and fibrils. Aβ oligomers are soluble and may spread throughout the brain, while fibrils are insoluble and form amyloid plaques. Aβ oligomers are considered more toxic than fibrils and are implicated in synaptic dysfunction and memory loss. Aβ can bind to various receptors, including NMDAR, α7nAChR, p75NTR, LRP, PrPc, and mGluR5, which may contribute to neuronal toxicity. Aβ degradation is regulated by proteases such as neprilysin, endothelin-converting enzymes, insulin-degrading enzyme, and plasmin. Aβ transport across the blood-brain barrier is regulated by receptors such as RAGE and LRP-1. ApoE plays a role in Aβ transport, clearance, and aggregation. The accumulation of Aβ in the brain is a hallmark of AD, and understanding its structure and function is crucial for developing effective therapies.Amyloid beta (Aβ) is a peptide derived from the amyloid precursor protein (APP) through cleavage by β- and γ-secretases. Aβ accumulation in the brain is considered an early toxic event in Alzheimer's disease (AD), which is the most common form of dementia. The physiological and pathological forms of Aβ, as well as the mechanisms by which Aβ causes dementia, are not fully understood. Currently, there are no effective drugs to stop or reverse AD progression. This review discusses the structure, biological functions, and neurotoxicity of Aβ, potential receptors that interact with Aβ, and therapeutic strategies for AD. It also summarizes recent advances in Aβ-targeted therapies, including small molecules, vaccines, and antibodies against Aβ, as well as inhibitors of β- and γ-secretases, Aβ-degrading proteases, and tau protein inhibitors. The structure of Aβ is complex, with different conformations such as monomers, oligomers, protofibrils, and fibrils. Aβ oligomers are soluble and may spread throughout the brain, while fibrils are insoluble and form amyloid plaques. Aβ oligomers are considered more toxic than fibrils and are implicated in synaptic dysfunction and memory loss. Aβ can bind to various receptors, including NMDAR, α7nAChR, p75NTR, LRP, PrPc, and mGluR5, which may contribute to neuronal toxicity. Aβ degradation is regulated by proteases such as neprilysin, endothelin-converting enzymes, insulin-degrading enzyme, and plasmin. Aβ transport across the blood-brain barrier is regulated by receptors such as RAGE and LRP-1. ApoE plays a role in Aβ transport, clearance, and aggregation. The accumulation of Aβ in the brain is a hallmark of AD, and understanding its structure and function is crucial for developing effective therapies.