Tryptophan-glucosamine conjugates modulate tau-derived PHF6 aggregation at low concentrations.
作者: Paul AshimLi Wen-HaoViswanathan Guru KrishnaKumarArad EladMohapatra SatabdeeLi GaoJelinek RazGazit EhudLi Yan-MeiSegal Daniel
作者单位: 1School of Molecular Cell Biology & Biotechnology, Tel Aviv University, Tel Aviv 69978, Israel. dsegal@post.tau.ac.il.
刊名: Chemical communications (Cambridge, England), 2019, Vol.55 (97), pp.14621-14624
来源数据库: PubMed Journal
DOI: 10.1039/c9cc06868f
原始语种摘要: Glycosylation of amyloidogenic proteins enhances their solubility and reduces propensity for aggregation. We therefore, prepared tryptophan-glucosamine conjugates to modulate aggregation of tau-derived PHF6-peptide. Combined in vitro and in silico approaches indicated that these conjugates inhibited oligomerization and fibril formation of PHF6 and disrupted its preformed fibrils at very low concentration. These effects mainly arise from the glucopyranoside moiety.
全文获取路径: PubMed  (合作)
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来源刊物:
影响因子:6.378 (2012)

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关键词翻译
关键词翻译
  • conjugates 接合藻类
  • modulate 
  • concentrations 浓聚物
  • glucosamine 葡萄糖胺
  • derived 导生的
  • fibril 细纤维
  • tryptophan 色氨酸
  • disrupted 断线状
  • aggregation 聚集
  • moiety 一部分