|
服务
产品  
|
Β-Amyloid (12-28)
| 名称
|
Β-Amyloid (12-28)
|
| 别名
|
|
| 序列（单字母缩写）
|
VHHQKLVFFAEDVGSNK
|
| 序列（三字母缩写）
|
{Val}{His}{His}{Gln}{Lys}{Leu}{Val}{Phe}{Phe}{Ala}{Glu}{Asp}{Val}{Gly}{Ser}{Asn}{Lys}
|
| 基本描述
|
Aß (12–28) residues are the binding site for apolipoprotein E (apoE) on Aß. This sequence encompasses a hydrophobic domain (residues 14–21) and a ß-turn (residues 22–28) which place two hydrophobic domains of Aß 14 to 21 and 29 to 40/42 opposite each other, allowing for the assembly of Aß peptides into fibrils. The secondary structure of Aß (12- 28), a neutral peptide, is dominated by α-helix and random coil. The interaction of apoE with residues 12 to 28 of Aß is not just a non-specific hydrophobic interaction but plays a pivotal role in the mechanism of Aß pathology in Alzheimer’s disease (AD). Beta-amyloid (12-28) and five other fragments enhanced aggregation of full length Aß (1-40). All of the peptides that enhance aggregation contained either residues 17 to 20 or 30 to 35, indicating the importance of these regions for promoting aggregation of full-length Aß.
|
| 分子量
|
1955.190
|
| 化学式
|
C89H135N25O25
|
| 纯度
|
> 95%
|
| 存储条件
|
Store β-amyloid (12-28) at -20°C.
|
| 注释
|
|
| Documents
|
|
| Figures
|
|
| Reference
|
|
|
