波谱学杂志 ›› 2009, Vol. 26 ›› Issue (4): 492-496.

• 4 • 上一篇    下一篇

阿尔茨海默氏症致病蛋白-Aβ(12-28) 肽段的NMR研究

  

  1. 中国科学院 上海药物研究所, 上海 201203
  • 收稿日期:2009-06-01 修回日期:2009-07-17 出版日期:2009-12-05 发布日期:2009-12-05

NMR Study of Aβ(12-28) Peptide from Alzheimer’s Disease

  1. Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China
  • Received:2009-06-01 Revised:2009-07-17 Online:2009-12-05 Published:2009-12-05

摘要:

Aβ肽的多聚化和纤维化在阿尔茨海默氏症(Alzheimer's diseas)的发生中起关键作用, 其中以Aβ(1-42) 的致病作用为最强,因此阻断其聚集成为阿尔茨海默氏症一种潜在的治疗方式. 作者在研究中发现某些化合物可以结合于Aβ(12-28) 肽段. 该文采用1H-1H COSY、TOCSY、ROESY和15N-HSQC多种核磁分析方法, 对此肽段的1H和15N NMR谱信号进行了归属和详细分析,为进一步研究其与小分子抑制剂的相互作用提供了基础.

关键词: 核磁共振(NMR), 信号归属,  , 2D NMR谱,  , A&beta, (12-28) 肽段

Abstract:

Oligomerization of Aβ peptides and fibril formation play critical roles in the pathology of Alzheimer’s disease (AD). Aβ(1-42) is the most toxic species of the  Aβ peptides. Disruption of Aβ aggregation is a promising approach in developing therapeutics for AD. In our previous studies, some compounds were found to be able to bind to Aβ(12-28). In this work, two-dimensional NMR methods were used to assign the 1H and 15N chemical shifts of Aβ(12-28) peptide. The results should provide a basis for the interaction study of Aβ(12-28) peptide with small molecule inhibitors.

Key words: NMR, signal assignment, 2D NMR, (12-28) peptide

中图分类号: