β-Amyloid (1-42), human, HFIP-treated 

β-Amyloid (1-42), human, HFIP-treated, a 42-amino acid peptide that has been treated with HFIP from β-Amyloid (1-42), human (HY-P1363A), is a brain-penetrant amyloid protein fragment, which can be used in research on Alzheimer's disease and Down’s syndrome. β-Amyloid (1-42), human, HFIP-treated remaining as a monomer exhibits antioxidant and neuroprotective effects. β-Amyloid (1-42), human, HFIP-treated, after being dissolved in DMSO to form the stock solution, on the one hand, can form soluble oligomers (AβOs) when incubated at 4°C, which have synaptic toxicity and neurotoxicity; on the other hand, it can be incubated at 37°C to form insoluble fibrils, with lower neurotoxicity, and participating in the oxidative damage process. Aβ42 oligomers bind to various neuronal surface receptors (such as PrPc, mGluR5, NMDA receptors, etc.), triggering oxidative stress, calcium homeostasis imbalance, and synaptic toxicity via activating downstream signaling pathways, leading to neuronal dysfunction and death^{[1][2][3][4][5][6][7]}.

β-Amyloid Aggregation Guidelines (Following is our recommended protocol. This protocol only provides a guideline, and should be modified according to your specific needs of your downstream experimental schemes). Oligomer preparation
1. β-Amyloid (1-42), human, treated with HFIP is dissolved in anhydrous DMSO/0.1M NaOH/1% ammonia solution at 5 mM. Then, dilute it with sterile double-distilled water to a certain concentration (eg: 200 μM) to ensure complete dissolution.
2. Next, the solution is age 24-48 h at 4-8°C. The sample is then centrifuged at 14000g for 10 min at 4-8°C; the soluble oligomers are in the supernatant. The supernatant is diluted 10-200-fold for experiments.
Fiber preparation:
1. β-Amyloid (1-42), human, treated with HFIP is dissolved in anhydrous DMSO at 5 mM and then dilutes into the appropriate concentration and buffer (10 mM HCl) with vortexing.
2. Next, the solution is age 24-48 h at 37°C to obtain Aβ42 fibrils.
Note:
1) If using PBS for dilution, it may cause the precipitation of the polypeptide.
2) The aggregation form is unstable in the solution, it is recommended to prepare and use it immediately. If storage is required, it is recommended to store the peptides in a film form at -20°C or -80°C.

β-Amyloid (1-42), human, HFIP-treated is prepared into oligomers, exhibiting neurotoxicity:
β-amyloid (1–42) peptide (60-180 μM, 48 h) could form oligomers significantly faster than Aβ40 and Aβ43 and Aβ42 oligomers (1-1000 μg/mL, 48 h) showed the greatest level of neurotoxicity in both SH-SY5Y and PC12 cells^[10].
Aβ42 oligomers (20 μM, 0-48 h) induces both apoptosis and autophagy in SH-SY5Y cells but only autophagy in U87 cells^[11].
Aβ42 oligomers (0.5 μM, 1 h) induces intracellular Ca²⁺ influx, mitochondrial reactive oxygen species (ROS) production and increases cell death in mouse neuroblastoma N2a cells^[12].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

Note:
Please do not refer to only one article to determine the experimental conditions. It is recommended to determine the optimal experimental conditions (animal strain, age, dosage, frequency and cycle, detection time and indicators, etc.) through preliminary experiments before the formal experiment.

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

4514.04

C₂₀₃H₃₁₁N₅₅O₆₀S

107761-42-2

Film

Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val-Ile-Ala

DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA

Shipping with dry ice.

Please store the product under the recommended conditions in the Certificate of Analysis.

* Please refer to the solubility information to select the appropriate solvent. The compound is unstable in solutions, freshly prepared is recommended.

• [1]. Solntseva EI, et al. Impact of amyloid-β peptide (1-42) on voltage-gated ion currents in molluscan neurons. Bull Exp Biol Med. 2011 Oct;151(6):671-4.  [Content Brief]

  [2]. Barucker C, et al. Nuclear translocation uncovers the amyloid peptide Aβ42 as a regulator of gene transcription. J Biol Chem. 2014 Jul 18;289(29):20182-91.  [Content Brief]

  [3]. Stefania Sabella, et al. Capillary electrophoresis studies on the aggregation process of beta-amyloid 1-42 and 1-40 peptides. Electrophoresis. 2004 Oct;25(18-19):3186-94.  [Content Brief]

  [4]. Porzoor A, et al. Pretreatment of chemically-synthesized Aβ42 affects its biological activity in yeast. Prion. 2014;8(6):404-10.  [Content Brief]

  [5]. Zou K, et al. A novel function of monomeric amyloid beta-protein serving as an antioxidant molecule against metal-induced oxidative damage. J Neurosci. 2002 Jun 15;22(12):4833-41.  [Content Brief]

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  [7]. Yao ZX, et al. Function of beta-amyloid in cholesterol transport: a lead to neurotoxicity. FASEB J. 2002 Oct;16(12):1677-9.  [Content Brief]

  [8]. Jancsó G, et al. Beta-amyloid (1-42) peptide impairs blood-brain barrier function after intracarotid infusion in rats. Neurosci Lett. 1998 Sep 4;253(2):139-41.  [Content Brief]

  [9]. Bourgade K, et al. β-Amyloid peptides display protective activity against the human Alzheimer's disease-associated herpes simplex virus-1. Biogerontology. 2015 Feb;16(1):85-98.  [Content Brief]

  [10]. Fu L, et al. Comparison of neurotoxicity of different aggregated forms of Aβ40, Aβ42 and Aβ43 in cell cultures. J Pept Sci. 2017 Mar;23(3):245-251.  [Content Brief]

  [11]. Wang H, et al. Amyloid-beta1-42 induces reactive oxygen species-mediated autophagic cell death in U87 and SH-SY5Y cells. J Alzheimers Dis. 2010;21(2):597-610.  [Content Brief]

  [12]. Fei X, et al. Degradation of FA reduces Aβ neurotoxicity and Alzheimer-related phenotypes. Mol Psychiatry. 2021 Oct;26(10):5578-5591.  [Content Brief]