Monitoring the aggregation of amyloid-prone proteins is critical for understanding the mechanism of amyloid fibril formation. Insulin, when dissolved in low pH buffer, has a surface tension of 61–64 mN m⁻¹, as measured by the pendant drop technique. Formation of insulin amyloid fibrils resulted in the increase of the surface tension values up to 71.2–73.5 mN m⁻¹. The kinetics of fibril formation and fibril morphology were validated by ThT fluorescence and AFM, respectively. The results demonstrate that monitoring the surface tension by the pendant drop technique is a valuable tool for the detection of insulin amyloid aggregation.

中文翻译：

---

通过悬滴技术监测表面张力以检测胰岛素原纤维形成

监测淀粉样蛋白的聚集对于了解淀粉样原纤维形成的机制至关重要。胰岛素，当溶解在低 pH 缓冲液中时，具有 61–64 mN m ^-1的表面张力，通过悬滴技术测量。胰岛素淀粉样蛋白原纤维的形成导致表面张力值增加至 71.2–73.5 mN m ^-1。原纤维形成的动力学和原纤维形态分别通过 ThT 荧光和 AFM 进行验证。结果表明，通过悬滴技术监测表面张力是检测胰岛素淀粉样蛋白聚集的宝贵工具。