人源 Beta Amyloid 1-40 | Aβ 40 的文献引用与应用实例

人源 Beta Amyloid 1-40 的文献引用与应用实例

The abnormal accumulation of amyloid-β (Aβ) peptide in the brain is one of the most important hallmarks of Alzheimer's disease. Aβ is an aggregation-prone and toxic polypeptide with 39–43 residues, derived from the amyloid precursor protein proteolysis process. According to the amyloid hypothesis, abnormal accumulation of Aβ in the brain is the primary influence driving Alzheimer's disease pathologies. Among all kinds of Aβ isoforms, Aβ40 and Aβ42 are believed to be the most important ones. Although these two kinds of Aβ differ only in two amino acid residues, recent studies show that they differsignificantly in their metabolism, physiological functions, toxicities, and aggregation mechanism.

淀粉样蛋白-β（Aβ）肽在大脑中的异常积聚是阿尔茨海默病最重要的标志之一。Aβ是一种易聚集的有毒多肽，具有39–43个残基，来源于淀粉样蛋白前体蛋白水解过程。根据淀粉样蛋白假说，Aβ在大脑中的异常积聚是导致阿尔茨海默病病理的主要影响因素。在各种Aβ亚型中，Aβ40和Aβ42被认为是最重要的亚型。尽管这两种Aβ仅在两个氨基酸残基上不同，但最近的研究表明，它们在代谢、生理功能、毒性和聚集机制方面存在显著差异。

Beta-amyloid production results from cleavage in the extracellular domain of APP by the beta-secretase (BACE1) , which results in the production of the APP C-terminal fragment C99. This fragment is further cleaved by the gamma-secretase at residues 40-42 to produce beta-amyloid 40 and 42 peptides. Beta-amyloid aggregation and neuritic plaque formation are pathologic hallmarks of Alzheimer disease. This peptide corresponds to the human beta-amyloid 1-40 peptide.

β-淀粉样蛋白的产生源于β分泌酶（BACE1）在APP的细胞外结构域中的切割，这导致APP C末端片段C99的产生。该片段在残基40-42处被γ分泌酶进一步切割以产生β-淀粉样蛋白40 和 42肽。β淀粉样蛋白聚集和神经炎斑块形成是阿尔茨海默病的病理特征。该肽对应于人β淀粉样蛋白1-40肽。

英文别名： Beta Amyloid 1-40 | Aβ40 | Aβ 1-40 | Abeta 40 | Abeta 1-40 | Amyloid-β 40 | β-Amyloid 1-40
中文名： β-淀粉样多肽 1-40 | Beta-淀粉样多肽 1-40 | Beta-淀粉样多肽 -40 | β-淀粉样多肽(1-40) | Beta-Amyloid多肽(1-40)
纯度： >95% by HPLC
序列(单字母)： DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV
(三字母序列)： 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
CAS No.： 131438-79-4
分子式： C194H295N53O58S1
分子量： 4329.90

文献引用：

文章：Peptide–surfactant interactions: Consequences for the amyloid-beta structure

作者：Sandra Rocha, Joana A. Loureiro, Gerald Brezesinski, Maria do Carmo Pereira

期刊：Biochemical and Biophysical Research Communications > 2012 > 420 > 1 > 136-140

文章链接：DOI：10.1016/j.bbrc.2012.02.129

Abstract

The conformation of amyloid-beta peptide (Aβ) determines if toxic aggregates are formed. The peptide structure by its turn depends on the environment and molecule–molecule interactions. We characterized the secondary structure of Aβ-(1–40) in surfactant solutions and interacting with monolayers. The peptide adopts β-sheet structure in solutions of ionic surfactants at sub-micelle concentrations and α-helix in the presence of ionic micelles. Uncharged micelles
induce β-sheets. Aβ-(1–40) alters the critical micelle concentration value of the non-ionic surfactant, underlining hydrophobic interactions. At ionic monolayers the peptide forms β-sheets when its concentration at the surface is high enough. These results suggest that only electrostatic interactions of charged micelles that surround completely the peptide are able to induce non-aggregated α-helix structure.

淀粉样蛋白β肽（Aβ）的构象决定了是否形成毒性聚集体。肽的结构取决于环境和分子之间的相互作用。我们表征了Aβ-（1-40）在表面活性剂溶液中的二级结构以及与单层的相 互作用。在亚胶束浓度的离子表面活性剂溶液中，肽采用β-片状结构，在离子胶束存在的情况下，肽采用α-螺旋结构。未充电的胶束诱导β-片。β-（1-40）改变了非离子表面 活性剂的临界胶束浓度值，突出了疏水相互作用。在离子单层中，当肽在表面的浓度足够高时，肽形成β-片。这些结果表明，只有完全包围肽的带电胶束的静电相互作用才能诱导 非聚集的α-螺旋结构。

产品链接：http://www.genicbio.cn/detail.html?article_id=87

关键词：Amyloid β-Peptide (1-40) human,TFA; Aβ1-40; β-Amyloid (1-40); Amyloid β-Peptide (1-40) human,TFA供应商, Amyloid抑制剂; 购买Amyloid β-Peptide (1-40) human,TFA; Amyloid β-Peptide (1-40) human,TFA溶解度; Amyloid β-Peptide (1-40) human,TFA结构式; Abeta 40; Aβ1-40; β-淀粉样多肽 1-40; Beta-淀粉样多肽1-40; Beta-淀粉样多肽 -40; β-淀粉样多肽(1-40); Beta-Amyloid多肽(1-40); Beta amyloid 1-40; Beta-amyloid 1-40; 131438-79-4