Amyloid-β

β-Amyloid (17-40) is a fragment of the Amyloid-β peptide that primarily targets neurotoxic pathways associated with Alzheimer's disease. This compound has demonstrated notable neurotoxic effects in SH-SY5Y and IMR-32 neuronal cell lines. Due to its biological activity, β-Amyloid (17-40) is a valuable tool for investigating the mechanisms underlying neurological diseases and for developing potential therapeutic strategies.

CTS-21166 is a selective inhibitor of β-site amyloid precursor protein cleaving enzyme 1 (BACE1), designed to penetrate the blood-brain barrier effectively. It demonstrates the ability to reduce levels of amyloid-beta (Aβ) in the brain, making it a valuable tool for studying the pathogenesis of Alzheimer's disease. CTS-21166 is suitable for use in both in vitro and in vivo research applications focused on Alzheimer's and related neurodegenerative disorders.

(Gly22)-Amyloid β-Protein (1-42) is a peptide fragment of the amyloid β-protein (Aβ) with a specific mutation at Glu22 to Gly22. This modification enhances the aggregation tendency of Aβ, a key component in the formation of amyloid plaques associated with Alzheimer's disease. Research applications include studying the molecular mechanisms of amyloid aggregation and evaluating potential therapeutic strategies for Alzheimer's disease.

β-Amyloid (10-35), amide targets amyloid-β, a key player in the pathogenesis of Alzheimer’s disease. Comprising 26 amino acids derived from the 10-35 region of the Aβ peptide, this reagent is critical for studying the aggregation and deposition of amyloid plaques. It is valuable for research applications focused on neurodegeneration, protein misfolding, and Alzheimer's pathology.

YIAD-0205 is an orally bioavailable inhibitor of amyloid-β (Aβ) aggregation, specifically targeting Aβ(1-42). This compound exhibits significant in vivo efficacy in a transgenic mouse model of Alzheimer's disease carrying five familial mutations (5XFAD). Its application lies in Alzheimer's research, particularly in studies exploring therapeutic strategies aimed at mitigating Aβ-related neurodegeneration.

Amyloid β-Protein (5-42) is an Aβ fragment that plays a critical role in the formation of amyloid plaques, a pathological hallmark of Alzheimer's disease. This peptide exhibits neurotoxic properties and serves as a key research tool in studies investigating the mechanisms underlying amyloid aggregation and neurodegeneration. It is commonly utilized to evaluate potential therapeutic agents aimed at mitigating Alzheimer's disease-related cognitive decline.

Aβ-IN-3 is a potent inhibitor of amyloid β (Aβ) aggregation, specifically targeting Aβ42. This compound effectively inhibits the aggregation of Aβ42, making it a valuable tool in the study of amyloid-related pathologies. However, Aβ-IN-3 does not mitigate the neurotoxicity associated with Aβ42 in SH-SY5Y cells, nor does it alter the aggregation state of Aβ42 into a non-toxic form. Its primary applications lie in research focused on Alzheimer's disease and amyloid aggregation mechanisms.

Dehydro nicardipine, a metabolite of Nicardipine, belongs to the dihydropyridine class of compounds. This compound selectively inhibits the aggregation of amyloid-beta (Aβ) monomers and regulates the extension and binding of soluble Aβ aggregates. Additionally, it alters the morphology of Aβ aggregates and inhibits their growth in length. Dehydro nicardipine is valuable for research applications focused on Alzheimer's disease.

PPI-1019 is an amyloid beta (Aβ) inhibitor that specifically targets the aggregation of Aβ peptides. This compound demonstrates potential neuroprotective effects, making it a valuable tool for researching neurodegenerative disorders, particularly Alzheimer's disease. Its role in modulating Aβ-related toxicity makes PPI-1019 significant for studies aimed at understanding the pathophysiology of amyloid plaque formation and developing therapeutic strategies.

β-Amyloid (1-9) is an N-terminal fragment of the amyloid-β peptide that encompasses amino acid residues 1 to 9. This fragment contains a B cell epitope, making it valuable for immunological studies. Although it lacks T cell epitopes, β-Amyloid (1-9) remains capable of forming amyloid fibrils and does not diminish fibril polymorphism when removed from the full-length Alzheimer's amyloid-β peptide (1-40). This specificity makes it useful for research into Alzheimer’s disease and related neurodegenerative conditions.

(Lys22)-Amyloid β-Protein (1-42) is a modified variant of the wild-type Amyloid β-Protein (1-42) peptide, featuring a lysine substitution at position 22. This mutation enhances the peptide's propensity to interact with molecular targets involved in Alzheimer’s disease pathology. It is essential for studies investigating amyloid aggregation, neurotoxicity, and the design of potential therapeutic agents for neurological disorders.

Aβ-IN-6 is an Aβ oligomers formation inhibitor that effectively reduces pro-inflammatory cytokine release from microglia. This compound significantly promotes Nrf2 nuclear translocation, thereby interfering with the aggregation of Aβ oligomers. Aβ-IN-6 offers neuroprotective effects through modulation of redox-sensitive signaling pathways in in vivo oxidative stress models. Its oral bioactivity and combined anti-inflammatory, antioxidant, and anti-oligomeric properties make Aβ-IN-6 a valuable reagent for research into Alzheimer's disease.

(Gln22)-Amyloid β-Protein (1-42) is a variant of β-Amyloid (1-42) featuring the Dutch mutation (E22Q). This modified peptide demonstrates increased fibrillogenic and pathogenic characteristics, making it essential for studying amyloidogenesis and its implications in neurodegenerative diseases. Research applications include investigations into Alzheimer's disease mechanisms and the assessment of potential therapeutic interventions targeting amyloid aggregation.

Dihydroergocristine mesylate is a potent inhibitor of γ-secretase, targeting the enzyme responsible for the generation of amyloid-β peptides implicated in Alzheimer’s disease. It effectively reduces the production of these peptides by binding directly to γ-secretase and Nicastrin, exhibiting equilibrium dissociation constants (Kd) of 25.7 nM and 9.8 μM, respectively. This compound can be utilized in research aimed at unraveling the mechanisms of Alzheimer’s pathology and developing potential therapeutic strategies.