Interaction between amyloid β-protein aggregates and membranes
Interaction between amyloid β-protein aggregates and membranes
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DOI：
10.1002/psc.570
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发表时间：
2004-10-01
影响因子：
2.1
通讯作者：
Matsuzaki, K
中科院分区：
文献类型：
--
作者：
Kakio, A;Yano, Y;Matsuzaki, K
可溶性、无毒的淀粉样β-蛋白（Abeta）转化为富含β-折叠结构的聚集的、有毒的A，被认为是阿尔茨海默病发展的关键步骤。因此，人们对 Abeta 聚集的机制以及在模拟生物液体的水溶液中形成的 Abeta 聚集体的表征进行了广泛的研究。另一方面，一些研究人员指出膜在 Abeta 聚集中发挥着重要作用。然而，目前尚不清楚溶液中形成的 Abeta 聚集体与膜中形成的 Abeta 聚集体是否相同以及前者是否可以与膜结合。在本研究中，使用染料标记的 Abeta-(1-40) 以及天然 Abeta-(1-40)，比较了在缓冲液和由单唾液酸神经节苷脂 GM1/胆固醇/鞘磷脂组成的筏状膜中形成的 Abeta 聚集体的特性。傅里叶变换红外光谱测量表明，缓冲液和膜中形成的 Abeta 聚集体具有不同的 β-折叠结构。荧光实验表明，缓冲液中聚集的 Abeta 对膜没有任何亲和力。版权所有 (C) 2004 欧洲肽协会和 John Wiley Sons, Ltd.
The conversion of soluble, nontoxic amyloid beta-protein (Abeta) to aggregated, toxic A rich in beta-sheet structures is considered to be the key step in the development of Alzheimer's disease. Therefore, extensive studies have been carried out on the mechanisms involved in Abeta aggregation and the characterization of Abeta aggregates formed in aqueous solutions mimicking biological fluids. On the other hand, several investigators pointed out that membranes play an important role in Abeta aggregation. However, it remains unclear whether Abeta aggregates formed in solution and membranes are identical and whether the former can bind to membranes. In this study, using a dye-labeled Abeta-(1-40) as well as native Abeta-(1-40), the proper-ties of Abeta aggregates formed in buffer and raft-like membranes composed of monosialoganglioside GM1/cholesterol/sphingomyelin were compared. Fourier transform infrared spectroscopic measurements suggested that Abeta aggregates formed in buffer and in membranes have different beta-sheet structures. Fluorescence experiments revealed that Abeta aggregated in buffer did not show any affinity for membranes. Copyright (C) 2004 European Peptide Society and John Wiley Sons, Ltd.