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Collapsed state of polyglutamic acid results in amyloid spherulite formation

机译：聚谷氨酸的塌陷状态导致淀粉样球晶的形成

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Self-assembly of proteins and peptides into amyloid fibrils involves multiple distinct intermediates and late-stage fibrillar polymorphs. Understanding the conditions and mechanisms that promote the formation of one type of intermediate and polymorph over the other represents a fundamental challenge. Answers to this question are also of immediate biomedical relevance since different amyloid aggregate species have been shown to have distinct pathogenic potencies. One amyloid polymorph that has received comparatively little attention are amyloid spherulites. Here we report that self-assembly of the intrinsically disordered polymer poly(L-glutamic) acid (PLE) can generate amyloid spherulites. We characterize spherulite growth kinetics, as well as the morphological, optical and tinctorial features of this amyloid polymorph previously unreported for PLE. We find that PLE spherulites share both tinctorial and structural characteristics with their amyloid fibril counterparts. Differences in PLE's molecular weight, polydispersity or chemistry could not explain the selective propensity toward either fibril or spherulite formation. Instead, we provide evidence that PLE polymers can exist in either a collapsed globule or an extended random coil conformation. The collapsed globule consistently produces spherulites while the extended coil assembles into disordered fibril bundles. This results suggests that these 2 PLE conformers directly affect the morphology of the resulting macroscopic amyloid assembly.
机译：蛋白质和多肽自组装成淀粉样原纤维涉及多个不同的中间体和后期原纤维多晶型物。了解促进一种类型的中间体和多晶型物形成另一种形式的条件和机理是一项根本性挑战。这个问题的答案也具有直接的生物医学意义，因为不同的淀粉样蛋白聚集体已被证明具有不同的致病力。一种受到较少关注的淀粉状多晶形物是淀粉状球晶。在这里我们报告，固有无序的聚合物聚（L-谷氨酸）酸（PLE）的自组装可以生成淀粉样球晶。我们表征了球状晶体的生长动力学，以及这种淀粉状多晶型物的形态，光学和着色特征，以前从未报道过PLE。我们发现PLE球晶与它们的淀粉样蛋白原纤维具有相同的着色和结构特征。 PLE的分子量，多分散性或化学性质的差异不能解释对原纤维或球晶形成的选择性倾向。取而代之的是，我们提供的证据表明PLE聚合物可以以塌陷的小球或扩展的无规卷曲构象存在。塌陷的球始终产生球晶，而延伸的线圈组装成无序的原纤维束。该结果表明，这两个PLE构象异构体直接影响所得的宏观淀粉样蛋白组装体的形态。

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