Chirality is ubiquitous in nature and plays crucial roles in biology, medicine, physics and materials science. Understanding and controlling chirality is therefore an important research challenge with broad implications. Unlike other chiral colloids, such as nanocellulose or filamentous viruses, amyloid fibrils form nematic phases but appear to miss their twisted form, the cholesteric or chiral nematic phases, despite a well-defined chirality at the single fibril level. Here we report the discovery of cholesteric phases in amyloids, using β-lactoglobulin fibrils shortened by shear stresses. The physical behaviour of these new cholesteric materials exhibits unprecedented structural complexity, with confinement-driven ordering transitions between at least three types of nematic and cholesteric tactoids. We use energy functional theory to rationalize these results and observe a chirality inversion from the left-handed amyloids to right-handed cholesteric droplets. These findings deepen our understanding of cholesteric phases, advancing their use in soft nanotechnology, nanomaterial templating and self-assembly.

手性在自然界无处不在，在生物学，医学，物理学和材料科学中起着至关重要的作用。因此，理解和控制手性是一项具有广泛意义的重要研究挑战。与其他手性胶体（例如纳米纤维素或丝状病毒）不同，淀粉样蛋白原纤维形成向列相，但似乎错过了它们的扭曲形式，即胆甾型或手性向列相，尽管在单个原纤维水平上具有明确的手性。在这里，我们报告使用β的淀粉样蛋白中胆甾相的发现-乳球蛋白原纤维因剪切应力而缩短。这些新型胆甾型材料的物理行为表现出空前的结构复杂性，在至少三种类型的向列型和胆甾型触觉体之间具有限制驱动的有序过渡。我们使用能量泛函理论使这些结果合理化，并观察到从左手淀粉样蛋白向右手胆甾型液滴的手性反转。这些发现加深了我们对胆甾相的理解，从而促进了它们在软纳米技术，纳米材料模板化​​和自组装中的应用。