Pentapeptide amides interfere with the aggregation of β-amyloid peptide of Alzheimer's disease
Pentapeptide amides interfere with the aggregation of β-amyloid peptide of Alzheimer's disease
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DOI：
10.1006/bbrc.2002.6745
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发表时间：
2002-04-12
影响因子：
3.1
通讯作者：
Penke, B
中科院分区：
文献类型：
--
作者：
Hetényi, C;Szabó, Z;Penke, B
淀粉样肽（Amyloid peptides，Abeta）在阿尔茨海默病（Alzheimer's disease，AD）的发病机制中起重要作用。Abeta分子的聚集导致原纤维和斑块形成。原纤维形成同时是AD的标志物和间接原因。抑制Abeta的聚集可能是治疗这种疾病的现实疗法。β折叠破坏剂（BSB）是一种类型的原纤维形成抑制剂。第一批BSB肽由Tjernberg等人（1996）和Soto等人（1998）设计。这些五肽已经在体外和体内证明了它们的有效性。在本研究中，两个五肽酰胺的影响。这些化合物是通过使用淀粉样肽的C-末端序列作为模板而设计的。应用生物测定来证明效率。通过FT-IR光谱和分子模拟方法研究了作用模式。(C)2002 Elsevier Science（美国）。
Amyloid peptides (Abeta) play a central role in the pathogenesis of Alzheimer's disease (AD). The aggregation of Abeta molecules leads to fibril and plaque formation. Fibrillogenesis is at the same time a marker and an indirect cause of AD. Inhibition of the aggregation of Abeta could be a realistic therapy for the illness. Beta sheet breakers (BSBs) are one type of fibrillogenesis inhibitors. The first BSB peptides were designed by Tjernberg et al. (1996) and Soto et al. (1998). These pentapeptides have proved their efficiency in vitro and in vivo. In the present study, the effects of two pentapeptide amides are reported. These compounds were designed by using the C-terminal sequence of the amyloid peptide as a template. Biological assays were applied to demonstrate efficiency. Modes of action were studied by FT-IR spectroscopy and molecular modeling methods. (C) 2002 Elsevier Science (USA).