• 主题
高级搜索  >
历史搜索 清空历史
首页> 美国卫生研究院文献>Elsevier Sponsored Documents >Ganglioside lipids accelerate α-synuclein amyloid formation
【2h】

Ganglioside lipids accelerate α-synuclein amyloid formation

机译：神经节苷脂脂质促进α-突触核蛋白淀粉样蛋白形成

代理获取
本网站仅为用户提供外文OA文献查询和代理获取服务，本网站没有原文。下单后我们将采用程序或人工为您竭诚获取高质量的原文，但由于OA文献来源多样且变更频繁，仍可能出现获取不到、文献不完整或与标题不符等情况，如果获取不到我们将提供退款服务。请知悉。
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The deposition of α-synuclein fibrils is one hallmark of Parkinson's disease. Here, we investigate how ganglioside lipids, present in high amounts in neurons and exosomes, influence the aggregation kinetics of α-synuclein. Gangliosides, as well as, other anionic lipid species with small or large headgroups were found to induce conformational changes of α-synuclein monomers and catalyse their aggregation at mildly acidic conditions. Although the extent of this catalytic effect was slightly higher for gangliosides, the results imply that charge interactions are more important than headgroup chemistry in triggering aggregation. In support of this idea, uncharged lipids with large headgroups were not found to induce any conformational change and only weakly catalyse aggregation. Intriguingly, aggregation was also triggered by free ganglioside headgroups, while these caused no conformational change of α-synuclein monomers. Our data reveal that partially folded α-synuclein helical intermediates are not required species in triggering of α-synuclein aggregation.
机译：α-突触核蛋白原纤维的沉积是帕金森氏病的标志之一。在这里，我们研究神经元和外泌体中大量存在的神经节苷脂如何影响α-突触核蛋白的聚集动力学。发现神经节苷脂以及其他具有小或大头基的阴离子脂质种类可诱导α-突触核蛋白单体的构象变化，并在弱酸性条件下催化其聚集。尽管神经节苷脂的这种催化作用的程度稍高，但结果表明电荷相互作用在引发聚集方面比头基化学更重要。支持该想法的是，未发现具有大头基的不带电荷的脂质诱导任何构象变化并且仅弱地催化聚集。有趣的是，聚集还由游离神经节苷脂头基团触发，而这些未引起α-突触核蛋白单体的构象变化。我们的数据显示，部分折叠的α-突触核蛋白螺旋中间体不是触发α-突触核蛋白聚集所需的物质。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
代理获取

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号