aβ42 in 1

Aβ42-IN-1, compound 1v, is a novel, potent and orally active γ-secretase modulator (GSM). Aβ42-IN-1 potently reduced Aβ42 levels with an IC 50 value of 0.091 μM in cultured cells without inhibiting CYP3A4. Aβ42-IN-1 shows a sustained pharmacokinetic profile.

Aβ42-IN-1 free base (compound 1v), an orally active γ-secretase modulator with high brain exposure, effectively lowers Aβ42 levels with an IC50 of 0.091 μM, and significantly diminishes brain Aβ42 levels in mice. Given these properties, Aβ42-IN-1 free base represents a potential disease-modifying agent for Alzheimer's disease [1].

CES1-IN-42 (2,2-Dimethoxy-2-phenylacetophenone) is a photoinitiator that can be used to assist in cancer research.

β-Amyloid(1-42), human, Ala-13C3,15N trifluoroacetic acid is a β-Amyloid (1-42), human marked with 13C and 15N. This unprocessed HFIP peptide comprises 42 amino acids and is a brain-permeable amyloid fragment, useful for researching Alzheimer's and Down syndrome. In monomer form, β-Amyloid (1-42), human provides antioxidant and neuroprotective effects. Upon HFIP monomerization and DMSO solvent preparation, it forms soluble oligomers (AβOs) at 4°C, which exhibit synaptotoxicity and neurotoxicity, while at 37°C it forms insoluble fibrils with lower neurotoxicity, involved in oxidative damage. Aβ42 oligomers interact with neuronal surface receptors such as PrPc, mGluR5, and NMDA receptor, activating signaling pathways that induce oxidative stress, calcium imbalance, synaptotoxicity, leading to neuronal dysfunction and death.

Biotin-amyloid-β (1-42) peptide is an affinity probe that allows amyloid-β (1-42) (Aβ42) to be detected or immobilized through interaction with the biotin ligand. It has been used to identify Aβ42 interaction partners in rat hippocampal synaptosomal membranes.

Amyloid-β (1-42) (Aβ42) is a neurotoxic 42-amino acid protein fragment found in amyloid plaques in postmortem cerebral cortex from patients with Alzheimer's disease.1,2,3Aggregation of Aβ42 results in the formation of neurotoxic fibrils or globular oligomers.1Aβ42 accumulates in the brain of many transgenic mouse models of Alzheimer's disease and, in many models, the onset of amyloid deposition positively correlates with deficits in spatial learning and memory.4 1.Wolfe, M.S.Therapeutic strategies for Alzheimer's diseaseNat. Rev. Drug Discov.1(11)859-866(2002) 2.Iwatsubo, T., Odaka, A., Suzuki, N., et al.Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ42(43)Neuron13(1)45-53(1994) 3.Hardy, J.A., and Higgins, G.A.Alzheimer's disease: The amyloid cascade hypothesisScience256(5054)184-185(1992) 4.Jankowsky, J.L., and Zheng, H.Practical considerations for choosing a mouse model of Alzheimer's diseaseMol. Neurodegener.12(1)89(2017)

TAMRA-Amyloid-β (1-42) peptide is a fluorescently labeled peptide. Amyloid-β (1-42) (Aβ42) is a neurotoxic 42-residue protein fragment found in amyloid plaques in postmortem cerebral cortex from patients with Alzheimer's disease. Aggregation of Aβ42 results in the formation of neurotoxic fibrils or globular oligomers. TAMRA-Amyloid-β (1-42) peptide is a labeled form of Aβ42 containing carboxytetramethyl rhodamine (TAMRA), which displays excitation/emission maxima of 543/572 nm, respectively.

(Met(O)35)-Amyloid β-Protein (1-42) is the oxidized form of Methionine 35 in Aβ42, capable of producing an oligomer size distribution similar to Aβ40. This compound is utilized in Alzheimer's disease (AD) research [1].

(Glu20)-Amyloid β-Protein (1-42) represents a variant of amyloid β-protein (Aβ) that fibrillizes more slowly due to the Glu20 mutation, which diminishes Aβ42's tendency to aggregate and inhibits the accumulation of this slowly fibrillizing peptide. Amyloid β-protein is the principal constituent of amyloid deposits in the vascular system and brain parenchyma in Alzheimer's disease [1] [2].

LSD1-IN-42 (Compound 7ae) is an orally active LSD1 inhibitor that significantly suppresses LSD1 activity (IC50 = 0.08 μM). It reduces PD-L1 expression and enhances the tumor-killing effect of T cells. LSD1-IN-42 demonstrates notable anti-gastric cancer activity by inhibiting tumor cell invasion and migration.

Aβ1–42 aggregation inhibitor 2 (compound 7c) is a potent inhibitor of Aβ1-42 aggregation, playing a significant role in Alzheimer's disease research. It exhibits excellent antioxidant properties, metal ion chelation ability, reduces oxidative stress, and demonstrates neuroprotective and anti-neuroinflammatory activities.

Aβ1–42 aggregation inhibitor 3 (Compound 3b) is an inhibitor of acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE), with IC50 values of 1.634 μM and 0.0285 μM, respectively. It effectively prevents the aggregation of Aβ1-42 and is applicable for Alzheimer's disease (AD) research.

PARP1-IN-42 (Example 43 cis-a) is a PARP1 inhibitor with an IC50 of less than 10 nM. It is utilized in tumor research.

Human beta-amyloid protein 42 (1-7) is a bioactive chemical.

β-Amyloid (1-42), rat/mouse TFA is a 42-amino-acid polypeptide fragment that exhibits neurotoxicity to hippocampal slices and is commonly used to establish Alzheimer's disease models for related research.

ChE/Aβ1-42-IN-1 (compound 28) is a potent aggregation inhibitor of ChE and Aβ1-42 with excellent BBB permeability, exhibiting IC50 values of 0.062 μM for AChE, 0.767 μM for BuChE, and 1.227 μM for Aβ1-42 aggregation. ChE/Aβ1-42-IN-1 is a potent multi-targeted anti-Alzheimer's disease agent [1].

Compound 16 (hAChE/Aβ1-42-IN-1) is a potent inhibitor targeting both hAChE and Aβ1-42 aggregation, demonstrating considerable safety in hepG2 cell lines and excellent brain-blood barrier (BBB) penetration with a broad safety margin. This compound shows promise for Alzheimer's disease (AD) research [1].

HIV-1 inhibitor-42 (compound 5b) is a potent inhibitor of HIV-1 with an IC50 of 0.06 μM. It inhibits HIV-1 RT RNA-dependent DNA polymerase with an IC50 of 0.518 μM and DNA-dependent DNA polymerase with an IC50 of 0.072 μM.

Aβ1-42 aggregation inhibitor 1 effectively inhibits acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) with IC50 values of 2.64 μM and 1.29 μM, respectively. At 25 μM, it also reduces self-mediated Aβ1-42 aggregation by 51.29%, showcasing its potential for Alzheimer's disease research [1].

β-Amyloid (42-1), human TFA is an inactive form of the amyloid β peptide (1-42) composed of 42 amino acids, which plays a key role in the pathogenesis of Alzheimer's disease and is commonly used to establish Alzheimer's disease animal models.

(Met(O2)35)-Amyloid β-Protein (1-42) is a peptide [1].

(Nle35)-Amyloid β-Protein (1-42) ammonium is a peptide.

(Gly22)-Amyloid β-Protein (1-42), a peptide fragment of Amyloid β-Protein (Aβ), plays a crucial role in Alzheimer's disease by forming the main component of vascular and parenchymal amyloid deposits. The Glu22 to Gly22 mutation in Aβ is known to enhance aggregation [1] [2].

(D-Asp1)-Amyloid β-Protein (1-42), a peptide fragment of amyloid β-protein (Aβ), serves as the primary constituent of vascular and parenchymal amyloid deposits associated with Alzheimer's disease [1].