MOLECULAR BASIS FOR INSULIN FIBRIL ASSEMBLY

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 在一种罕见的称为注射淀粉样变性的疾病中，可以观察到胰岛素的细胞外纤维。我们发现，序列为LVEALYL的胰岛素B链片段是最小的片段，它以摩尔比依赖的方式既成核又抑制全长胰岛素的纤颤，这表明这一片段是胰岛素原纤维的交叉β脊椎的中心。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. In the rare medical condition termed injection amyloidosis, extracellular fibrils of insulin are observed. We found that the segment of the insulin B-chain with sequence LVEALYL is the smallest segment that both nucleates and inhibits the fibrillation of full-length insulin in a molar ratio-dependent manner, suggesting that this segment is central to the cross-beta spine of the insulin fibril.