Amyloid fibril formation by proteins and their deposition in cells and tissues are associated with several amyloid-based disorders. Understanding the mechanism of amyloid fibril formation is thus of the utmost importance for the designing ligands that could prevent or inhibit the fibrillation process and help to treat of such disorders. We describe the stimulatory effect of sodium dodecyl benzenesulfonate (SDBS) on insulin amyloid fibrillation at pH 2.0 and the characterization of SDBS-induced insulin aggregation using spectroscopy and microscopy. We found that SDBS induced amyloid-like aggregates of insulin at sub-micellar (0.1-1.2 mM), but not post-micellar (≥2.0 mM) concentrations. The amyloid fibrillation of insulin induced by SDBS was kinetically rapid and escaped the lag phase. Far-UV CD findings suggested that the α-helical content of insulin transformed into cross-β structure and mixed α and β structures when incubated with sub-micellar and post-micellar SDBS concentrations, respectively. The overall results indicated that low, but not high SDBS concentrations induce amyloid-like insulin aggregates and fibrils.

中文翻译：

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解析十二烷基苯磺酸钠表面活性剂的胶束和胶束浓度在pH 2.0时的胰岛素原纤化中的作用。

由蛋白质形成的淀粉样蛋白原纤维及其在细胞和组织中的沉积与几种基于淀粉样蛋白的疾病有关。因此，了解淀粉样蛋白原纤维形成的机制对于设计可预防或抑制原纤维形成过程并有助于治疗此类疾病的配体至关重要。我们描述了十二烷基苯磺酸钠（SDBS）在pH 2.0时对淀粉样蛋白原纤化的刺激作用以及使用光谱学和显微镜观察SDBS诱导的胰岛素聚集的特性。我们发现，SDBS在低于胶束（0.1-1.2 mM）的浓度下诱导了胰岛素的淀粉样蛋白样聚集体，但在胶束后（≥2.0mM）的浓度下却没有。SDBS诱导的胰岛素的淀粉样蛋白原纤维动力学动力学迅速并逃脱了滞后阶段。远紫外线CD的发现表明，当分别与亚胶束浓度和胶束后浓度的SDBS孵育时，胰岛素的α-螺旋含量会转变为交叉β结构以及混合的α和β结构。总体结果表明，低但不高的SDBS浓度会诱导淀粉样蛋白样胰岛素聚集体和原纤维。