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β-Amyloid 1-16(Amyloidβ-Protein(1-16))
本产品不向个人销售,仅用作科学研究,不用于任何人体实验及非科研性质的动物实验。
CAS NO:131580-10-4
规格:98%
分子量:1955.04
包装与价格:
包装价格(元)
1mg电议
5mg电议

产品介绍
β-Amyloid(1-16)是可参与金属结合的β-淀粉样蛋白片段。β-淀粉样蛋白是在阿尔茨海默病患者的脑中形成淀粉样斑块的肽。
CAS:131580-10-4
分子式:C84H119N27O28
分子量:1955.04
纯度:98%
存储:Store at -20°C

Background:

β-Amyloid (1-16) 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.



β-amyloid (1-16) 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. Oxidation targets for β-Amyloid (1-16) are the histidine residues coordinated to the metal ions. Copper is bound to Aβ in senile plaque of Alzheimer’s disease with β-Amyloid (1-16) taking part in the coordination of the Cu2+ ions. Cu2+ and Zn2+ are linked with the neurotoxicity of -Amyloid and free radical damage[1]. β-amyloid (1-16) is the minimal amino acidic sequence display a Cu coordination mode which involves three Histidines (His6, His13 and His14). β-amyloid (1-16) is supposed to be involved in metal binding[2]. Human β-amyloid interacts with zinc ions through its metal-binding domain 1-16. The C-tails of the two polypeptide chains of the rat Aβ(1-16) dimer are oriented in opposite directions to each other, which hinders the assembly of rat Aβ dimers into oligomeric aggregates. Thus, the differences in the structure of zinc-binding sites of human and rat β-Amyloid (1-16), their ability to form regular cross-monomer bonds, and the orientation of their hydrophobic C-tails could be responsible for the resistance of rats to Alzheimer’s disease[3].


[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. [2]. Minicozzi V, et al. Identifying the minimal copper- and zinc-binding site sequence in amyloid-beta peptides. J Biol Chem. 2008 Apr 18;283(16):10784-92. [3]. Istrate AN, et al. NMR solution structure of rat aβ(1-16): toward understanding the mechanism of rats’ resistance to Alzheimer’s disease. Biophys J. 2012 Jan 4;102(1):136-43.