中文摘要：

测试是否的摘要 IL-1 RI/My088-TIR 作为在堵住 MyD88 依赖的发信号的小径指向了的新混合物模仿 AS-1 罐头工作，我们调查了物理结构和 AS-1 的生物功能。AS-1 的结晶的结构被 1H 检验的方法原子磁性的回声。AS-1 的毒性与甲基 thiazolyl tetrazolium (MTT ) 被测量试金。p38 MAPK 和 IRAK-1 的 phosphorylation 状态上的 AS-1 的效果与西方的污点被观察。结果 AS-1 的结晶的细节证明它是一个 tri 肽序列[(F/Y ) IL-1R I-TIR 领域 BB 环的 -(V/L/I)-(P/G)] 。AS-1 的毒性都没被显示出到 HEK 293A 房间。p38 MAPK 的 phosphorylation，导致了由 IL-1significantly 在控制组从那些增加了。AS-1 显著地减少了 IL-1 导致的 p38 MAPK 的 phosphorylation。IL-1 显著地增加了 IRAK-1 的 phosphorylation，它被 AS-1 阻止。结论 AS-1 是一竞争在 IL-1R I-TIR 和 MyD88-TIR 领域之间模仿，它很可能防碍 MyD88 依赖的发信号小径。

英文摘要：

Objective： To test whether IL-1 RI/My088-TIR mimic AS-1 can work as a new compound that targeted at blocking MyD88- dependent signaling pathway, we investigated the physical structure and biological function of AS-1. Methods：The crystallographic structure of AS-1 was examined by 1^H nuclear magnetic resonance. The toxicity of AS-1 was measured with Methyl thiazolyl tetrazolium （MTT） assay. The effect of AS-1 on phosphorylation state of p38 MAPK and IRAK-1 was observed with Western blot. Results：The crystallographic details of AS-1 demonstrated that it was a tri-peptide sequence[（F/Y）-（V/L/I）-（P/G）] of the IL-1R I -TIR domain BBloop. No toxicity of AS-1 was shown to HEK 293A cells. The phosphorylation of p38 MAPK, induced by IL-1β significantly increased from those in the control group. AS-1 significantly reduced the phosphorylation of p38 MAPK induced by IL-1β. IL-1β increased the phosphorylation of IRAK-1 significantly, which was prevented by AS-1. Conclusion：AS-1 is a competitive mimic between IL-1R I-TIR and MyD88-TIR domain, which most likely interferes with MyD88-dependent signaling pathway.