β-Amyloid (1-28)  (Synonyms: Amyloid β-Protein (1-28))

β-Amyloid (1-28) is a β-Amyloid protein fragment involved in metal binding. Beta-amyloid is a peptide that forms amyloid plaques in the brains of Alzheimer's disease (AD) patients.

Amyloid-β^[1]

β-Amyloid Aggregation Guidelines (Following is our recommended protocol. This protocol only provides a guideline, and should be modified according to your specific needs).
1. Solid Aβ peptide was dissolved in cold hexafluoro-2-propanol (HFIP). The peptide was incubated at room temperature for at least 1h to establish monomerization and randomization of structure.
2. The HFIP was removed by evaporation, and the resulting peptide was stored as a film at -20 or -80 ℃.
3. The resulting film was dissolved in anhydrous DMSO at 5 mM and then diluted into the appropriate concentration and buffer (serum- and phenol red-free culture medium) with vortexing.
4. Next, the solution was age 48h at 4-8 ℃. The sample was then centrifuged at 14000g for 10 min at 4-8 ℃; the soluble oligomers were in the supernatant. The supernatant was diluted 10-200-fold for experiments.

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

β-Amyloid (1-28) fragment is considered as valid models to examine the contribution of the key histidine residues (His , His in mouse and His , His , His in human fragments) to the Ab–Cu²⁺ interaction^[1]. Copper binds to β-Amyloid (1-28) at pH 7.4 with an affinity of K_a10 ⁷ M^-1[2].

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

3262.51

C₁₄₅H₂₀₉N₄₁O₄₆

109770-29-8

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

DAEFRHDSGYEVHHQKLVFFAEDVGSNK

Room temperature in continental US; may vary elsewhere.

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

• [1]. Kowalik-Jankowska T, et al. Coordination abilities of the 1-16 and 1-28 fragments of beta-amyloid peptide towards copper(II) ions: a combined potentiometric and spectroscopic study. J Inorg Biochem. 2003 Jul 1;95(4):270-82.  [Content Brief]

  [2]. Syme CD, et al. Copper binding to the amyloid-beta (Abeta) peptide associated with Alzheimer's disease: folding, coordination geometry, pH dependence, stoichiometry, and affinity of Abeta-(1-28): insights from a range of complementary spectroscopic techni  [Content Brief]

  [3]. Jing-Ming Shi, et al. Dissecting the behaviour of β-amyloid peptide variants during oligomerization and fibrillation. J Pept Sci. 2017 Nov;23(11):810-817.  [Content Brief]