A6933
Acetyl-Amyloid β-Protein Fragment 15-20 Amide
≥97% (HPLC), powder
别名:
Ac-QKLVFF-NH2, amyloid blocker
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关于此项目
经验公式（希尔记法）:
C42H63N9O8
化学文摘社编号:
分子量:
822.01
MDL编号:
UNSPSC代码:
12352202
PubChem化学物质编号:
NACRES:
NA.32
质量水平
方案
≥97% (HPLC)
表单
powder
颜色
white
UniProt登记号
储存温度
−20°C
SMILES字符串
CC(C)C[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(N)=O)NC(C)=O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](Cc2ccccc2)C(N)=O
InChI
1S/C42H63N9O8/c1-25(2)22-33(49-38(55)30(18-12-13-21-43)47-39(56)31(46-27(5)52)19-20-35(44)53)41(58)51-36(26(3)4)42(59)50-34(24-29-16-10-7-11-17-29)40(57)48-32(37(45)54)23-28-14-8-6-9-15-28/h6-11,14-17,25-26,30-34,36H,12-13,18-24,43H2,1-5H3,(H2,44,53)(H2,45,54)(H,46,52)(H,47,56)(H,48,57)(H,49,55)(H,50,59)(H,51,58)/t30-,31-,32-,33-,34-,36-/m0/s1
InChI key
DDXTVYDSGCHGAN-PITCCTKHSA-N
基因信息
human ... APP(351)
Amino Acid Sequence
Ac-Gln-Lys-Leu-Val-Phe-Phe-NH2
生化/生理作用
Amyloid plaques characteristic of the Alzheimer brain contain fibrils composed of amyloid beta aggregates. Short peptides containing the sequence KLVFF have been shown to bind specifically to the homologous region in Aβ and are used to prevent full length amyloid fibril formation.
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
L O Tjernberg et al.
The Journal of biological chemistry, 271(15), 8545-8548 (1996-04-12)
Polymerization of amyloid beta-peptide (Abeta) into amyloid fibrils is a critical step in the pathogenesis of Alzheimer's disease. Here, we show that peptides incorporating a short Abeta fragment (KLVFF; Abeta16-20) can bind full-length Abeta and prevent its assembly into amyloid
L O Tjernberg et al.
The Journal of biological chemistry, 272(19), 12601-12605 (1997-05-09)
We have previously shown that short peptides incorporating the sequence KLVFF can bind to the approximately 40amino acid residue Alzheimer amyloid beta-peptide (Abeta) and disrupt amyloid fibril formation (Tjernberg, L. O., Näslund, J., Lindqvist, F., Johansson, J., Karlström, A. R.
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