摘要
Aβ肽的多聚化和纤维化在阿尔茨海默氏症(Alzhei mer'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-1HCOSY、TOC-SY、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.
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.
出处
《波谱学杂志》
CAS
CSCD
北大核心
2009年第4期492-496,共5页
Chinese Journal of Magnetic Resonance