Amyloid-β Peptide-Lipid Bilayer Interaction investigated by Supercritical Angle Fluorescence.

Amyloid-β Peptide-Lipid Bilayer Interaction investigated by Supercritical Angle Fluorescence.
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通过超临界角荧光研究淀粉样蛋白-β 肽-脂质双层相互作用。

DOI:
10.1021/acschemneuro.9b00264
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发表时间:
2019
影响因子:
5
通讯作者:
S. Seeger
S. Seeger
中科院分区:
医学3区
文献类型:
--
作者:
V. Dubois;Diana Serrano;S. Seeger

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了解神经元膜与β淀粉样蛋白肽之间的相互作用对于阐明阿尔茨海默病的毒性机制至关重要。本文介绍了如何应用超临界角荧光光谱实时监测支持的脂质双层(SLB)和肽之间的相互作用。测试了不同形式的淀粉样蛋白-β(40和42个氨基酸组成),并测量界面荧光以获得关于脂质完整性和流动性的信息。结果表明,脂质双层的浓度依赖性的损伤过程。与肽长达48小时的长时间相互作用导致脂质分子从表面提取和聚集,以及与肽聚集体形成相关的双层的潜在破坏。脂质的自然扩散受到与淀粉样蛋白-β(1 - 42)的相互作用的轻微阻碍,并且与肽的寡聚化密切相关。还根据亲和力表征了淀粉样蛋白-β的吸附和解吸。淀粉样蛋白-β(1 - 42)表现出比淀粉样蛋白-β(1 - 40)略高的亲和力。前者也更容易聚集和吸附在双层低聚物。
The understanding of the interaction between the membrane of neurons and Amyloid-β peptides is of crucial importance to shed light on the mechanism of toxicity in Alzheimer disease. This paper describes how supercritical angle fluorescence spectroscopy was applied to monitor in real-time the interaction between a supported lipid bilayer (SLB) and the peptide. Different forms of Amyloid-β (40 and 42 amino acids composition) were tested and the interfacial fluorescence was measured to get information about the lipid integrity and mobility. The results show a concentration-dependent damaging process of the lipid bilayer. Prolonged interaction with the peptide up to 48 hours lead to an extraction and clustering of lipid molecules from the surface and a potential disruption of the bilayer, correlated with the formation of peptide aggregates. The natural diffusion of the lipid was slightly hindered by the interaction with Amyloid-β(1-42) and closely related to the oligomerization of the peptide. The adsorption and desorption of Amyloid-β was also characterized in terms of affinity. Amyloid-β(1-42) exhibited a slightly higher affinity than Amyloid-β(1-40). The former was also more prone to aggregate and to adsorb on the bilayer as oligomer.
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