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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Effect of tert-alcohol functional imidazolium salts on oligomerization and fibrillization of amyloid beta (1-42) peptide
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Effect of tert-alcohol functional imidazolium salts on oligomerization and fibrillization of amyloid beta (1-42) peptide

机译:叔醇功能性咪唑鎓盐对淀粉样蛋白β(1-42)肽寡聚化和原纤化的影响

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摘要

Imidazolium based IL's has gained vast interest in developing biological applications. Oligomerization and fibrillization of amyloid beta (1-42) peptide are mainly responsible for the extra-neuronal deposition of amyloid fibrils in neurodegenerative disorders like Alzheimer's disease (AD). Here, we report an effect of tert-BuOH-functional imidazolium ILs on oligomerization and fibrillization of amyloid beta (1-42) Peptide in vitro. In this study, a series of these [alkyl-(t)OHim][OMs] ILs with methyl sulphonate counter anion by varying alkyl chains were used. Among the seven protic ILs, four showed strong binding and inhibition activity for the formation of amyloid beta (1-42) aggregation by using Thioflavin T fluorescence binding assay. The secondary structural analysis of the peptide, pre-incubated with active ILs shows the loss of ordered beta-sheet amyloid structure. The longer alkyl chain ILs showed that an increased in amyloid binding and hence an inhibition effect on amyloid aggregation was enhanced. Thus, we propose that ILs could be presented as potential candidates for therapeutic intervention against Alzheimer's disease (AD).
机译:基于Imidazolium的IL在开发生物学应用方面取得了巨大兴趣。淀粉样蛋白β(1-42)肽的寡聚和原纤化主要负责淀粉样蛋白原纤维的超神经元沉积,如阿尔茨海默病(AD)。这里,我们在体外报告了Tert-Buoh官能咪唑鎓ILs对淀粉样蛋白β(1-42)肽的寡聚化和原纤化的影响。在该研究中,使用通过改变烷基链的一系列具有甲磺酸甲酯对抗阴离子的[烷基 - (t)OHIM] [OMS] IL。在七种质子ILS中,通过使用硫蛋白T荧光结合测定,四个含有淀粉样蛋白β(1-42)聚集的强粘合和抑制活性。与活性ILS预孵育的肽的二次结构分析显示有序β-片状淀粉样蛋白结构的损失。较长的烷基链ILs显示淀粉样蛋白结合中的增加,因此提高了对淀粉样蛋白聚集的抑制作用。因此,我们提出了ILS可以作为针对阿尔茨海默病(AD)的治疗干预的潜在候选人。

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