纤维发生
肽
化学
纤维
共轭体系
生物化学
海藻糖
共价键
淀粉样蛋白(真菌学)
生物物理学
生物
有机化学
无机化学
聚合物
作者
Paolo De Bona,Maria Gabriella Giuffrida,Filippo Caraci,Agata Copani,Bruno Pignataro,Francesco Attanasio,Sebastiano Cataldo,Giuseppe Pappalardo,Enrico Rizzarelli
摘要
Aggregation of the amyloid Aβ peptide and its accumulation into insoluble deposits (plaques) are believed to be the main cause of neuronal dysfunction associated with Alzheimer's disease (AD); small molecules that can interfere with the Aβ amyloid fibril formation are therefore of interest for a potential therapeutic strategy. Three new trehalose-conjugated peptides of the well known β-sheet breaker peptide iAβ5p, were synthesized. The disaccharide was covalently attached to different sites of the LPFFD peptide chain, i.e. at the N-terminus, C-terminus or at the Asp side chain. CD spectroscopy in different solvents was used to assess changes in the peptide conformation of these compounds. The effects of these glycopeptides on the self-assembly and morphology of Aβ aggregates were investigated by ThT fluorescence assay and dynamic Scanning Force Microscopy, respectively. All the synthesized compounds were tested as inhibitors of Aβ toxicity toward pure cultures of rat cortical neurons. Copyright © 2009 European Peptide Society and John Wiley & Sons, Ltd.
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