A method is designed to quickly form protein hydrogels, based on the self-assembly of highly concentrated lysozyme solutions in acidic conditions. Their properties can be easily modulated by selecting the curing temperature. Molecular insights on the gelation pathway, derived by in situ FTIR spectroscopy, are related to calorimetric and rheological results, providing a consistent picture on structure–property correlations. In these self-crowded samples, the thermal unfolding induces the rapid formation of amyloid aggregates, leading to temperature-dependent quasi-stationary levels of antiparallel cross β-sheet links, attributed to kinetically trapped oligomers. Upon subsequent cooling, thermoreversible hydrogels develop by the formation of interoligomer contacts. Through heating/cooling cycles, the starting solutions can be largely recovered back, due to oligomer-to-monomer dissociation and refolding. Overall, transparent protein hydrogels can be easily formed in self-crowding conditions and their properties explained, considering the formation of interconnected amyloid oligomers. This type of biomaterial might be relevant in different fields, along with analogous systems of a fibrillar nature more commonly considered.

中文翻译：

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在拥挤的条件下溶菌酶的淀粉样自组装：蛋白质低聚物水凝胶的形成。

一种基于高浓度溶菌酶溶液在酸性条件下的自组装，可以快速形成蛋白质水凝胶的方法。通过选择固化温度，可以轻松调节其性能。通过原位FTIR光谱学获得的关于凝胶化途径的分子见解与量热和流变学结果相关，从而提供了结构-特性相关性的一致描述。在这些自拥挤的样品中，热展开诱导淀粉样蛋白聚集体的快速形成，从而导致温度平行平行β-折叠链平行的准静态水平，这归因于动力学捕获的低聚物。在随后的冷却中，通过形成低聚物间接触形成热可逆水凝胶。通过加热/冷却循环，可以大量回收起始溶液，由于低聚物到单体的解离和重折叠。总体而言，考虑到相互连接的淀粉样蛋白低聚物的形成，透明的蛋白质水凝胶很容易在自拥挤的条件下形成，并对其性质进行了解释。这种类型的生物材料可能与不同领域相关，以及更常见的具有纤维状性质的类似系统。