In order to achieve a comprehensive understanding of protein aggregation processes, an exploration of solvation dynamics, a key yet intricate component of biological phenomena, is mandatory. In the present study, we used Fourier transform infrared spectroscopy and terahertz spectroscopy complemented by atomic force microscopy and kinetic experiments utilizing thioflavin T fluorescence to elucidate the changes in solvation dynamics during liquid-liquid phase separation and subsequent amyloid fibril formation, the latter representing a transition from liquid to solid phase separation. These processes are pivotal in the pathology of neurodegenerative disorders such as Alzheimer’s and Parkinson’s diseases. We focus on the ACC1–13K24-ATP protein complex, which undergoes fibril formation followed by droplet generation. Our investigation reveals the importance of hydration as a driving force in these processes, offering new insights into the molecular mechanisms at play.

中文翻译：

---

用 ATP 揭示 ACC1-13K24 的水合动力学：从液体到液滴再到淀粉样蛋白原纤维


为了全面了解蛋白质聚集过程，必须探索溶剂化动力学，这是生物现象的一个关键而复杂的组成部分。在本研究中，我们使用傅里叶变换红外光谱和太赫兹光谱，并辅以原子力显微镜和利用硫黄素 T 荧光的动力学实验来阐明液-液相分离和随后的淀粉样蛋白原纤维形成过程中溶剂化动力学的变化，后者代表从液相分离到固相分离的转变。这些过程在神经退行性疾病（如阿尔茨海默病和帕金森病）的病理学中至关重要。我们专注于 ACC1-13K24-ATP 蛋白复合物，它经历原纤维形成，然后产生液滴。我们的研究揭示了水合作用作为这些过程中驱动力的重要性，为起作用的分子机制提供了新的见解。