• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Chemistry: A European journal >Cross-Talk Between the Octarepeat Domain and the Fifth Binding Site of Prion Protein Driven by the Interaction of Copper(II) with the N-terminus
【24h】

Cross-Talk Between the Octarepeat Domain and the Fifth Binding Site of Prion Protein Driven by the Interaction of Copper(II) with the N-terminus

机译：铜（II）与N末端的相互作用驱动八邻域域和Domain蛋白的第五个结合位点之间的交叉对话

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Prion diseases are a group of neurodegenerative diseases based on the conformational conversion of the normal form of the prion protein (PrPC) to the disease-related scrapie isoform (PrPSc). Copper(II) coordination to PrPC has attracted considerable interest for almost 20 years, mainly due to the possibility that such an interaction would be an important event for the physiological function of PrPC. In this work, we report the copper(II) coordination features of the peptide fragment Ac(PEG(11))(3)PrP(60-114) [Ac= acetyl] as a model for the whole N-terminus of the PrPC metal-binding domain. We studied the complexation properties of the peptide by means of potentiometric, UV/Vis, circular dichroism and electrospray ionisation mass spectrometry techniques. The results revealed that the preferred histidyl binding sites largely depend on the pH and copper(II)/peptide ratio. Formation of macrochelate species occurs up to a 2: 1 metal/peptide ratio in the physiological pH range and simultaneously involves the histidyl residues present both inside and outside the octarepeat domain. However, at increased copper(II)/peptide ratios amide-bound species form, especially within the octarepeat domain. On the contrary, at basic pH the amide-bound species predominate at any copper/peptide ratio and are formed preferably with the binding sites of His96 and His111, which is similar to the metal-binding-affinity order observed in our previous studies.
机译：on病毒是一组神经退行性疾病，基于正常形式的病毒蛋白（PrPC）向与疾病相关的瘙痒病亚型（PrPSc）的构象转化。铜（II）与PrPC的配位已引起近20年的关注，这主要是由于这种相互作用可能是PrPC生理功能的重要事件。在这项工作中，我们报告肽片段Ac（PEG（11））（3）PrP（60-114）[Ac =乙酰基]的铜（II）配位特征作为PrPC整个N端的模型金属结合域。我们通过电位，UV / Vis，圆二色性和电喷雾电离质谱技术研究了该肽的络合特性。结果表明，优选的组氨酸结合位点主要取决于pH和铜（II）/肽的比率。大螯合物物种的形成在生理pH范围内以高达2∶1的金属/肽比率发生，并且同时涉及存在于八叠域内部和外部的组氨酸残基。然而，随着铜（II）/肽比例的增加，形成酰胺结合的物种，尤其是在八面体域内。相反，在碱性pH下，酰胺键结合的物质在任何铜/肽比率下均占优势，并且优选与His96和His111的结合位点形成，这与我们先前研究中观察到的金属结合亲和力顺序相似。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

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