MOLECULAR BASIS FOR INSULIN FIBRIL ASSEMBLY

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 在称为注射性淀粉样变性的罕见医学病症中，观察到胰岛素的细胞外原纤维。我们发现，具有序列LVENUL的胰岛素B链片段是以摩尔比依赖性方式使全长胰岛素成核并抑制其原纤化的最小片段，这表明该片段是胰岛素原纤的交叉β棘的中心。

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.