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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Different effects of Alzheimer's peptide A￡(l-40) oligomers and fibrils on supported lipid membranes
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Different effects of Alzheimer's peptide A￡(l-40) oligomers and fibrils on supported lipid membranes

机译：阿尔茨海默氏症肽A ￡（l-40）低聚物和原纤维对支持的脂质膜的不同作用

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摘要

Beta-amyloid (1-40) is one of the two most abundant species of amyloid-beta peptides present as fibrils in the extracellular senile plaques in the brain of Alzheimer's patients. Recently, the molecular aggregates constituting the early stage of fibril formation, i.e., oligomers and protofibrils, have been investigated as the main responsible for amyloid-beta cytotoxic effect. The molecular mechanism leading to neurodegeneration is still under debate, and it is common opinion that it may reside in the interaction between amyloid species and the neural membrane. In this investigation Atomic Force Microscopy and spectroscopy have been used to understand how structural (and mechanical) properties of POPC/POPS lipid bilayers, simulating the phospholipid composition and negative net charge of neuritic cell membranes, are influenced by the interaction with Abeta(l-40), in different stages of the peptide aggregation. Substantial differences in the damage caused to the lipid bilayers have been observed, confirming the toxic effect exerted especially by Abeta(l-40) prefibrillar oligomers.
机译：β-淀粉样蛋白（1-40）是在阿尔茨海默氏病患者大脑中的细胞外老年斑中以原纤维形式存在的两种淀粉样蛋白-β肽中含量最高的一种。最近，已经研究了构成原纤维形成早期阶段的分子聚集体，即低聚物和原纤维，是造成β淀粉样蛋白细胞毒性作用的主要原因。导致神经变性的分子机制仍在争论中，并且普遍认为它可能存在于淀粉样物质与神经膜之间的相互作用中。在这项研究中，原子力显微镜和光谱学已被用来了解POPC / POPS脂质双层的结构（和机械）特性如何模拟神经细胞膜的磷脂成分和负净电荷，受到与Abeta（l- 40），处于肽聚集的不同阶段。已经观察到对脂质双层造成的损害的实质性差异，证实了尤其是由Abeta（1-40）原纤维低聚物发挥的毒性作用。

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