Department of Chemistry, KTH Royal Institute of Technology, Teknikringen 30, 100 44, Stockholm, Sweden.
Department of Molecular Sciences, Swedish University of Agricultural Sciences, BioCentrum, Almas Allé 5, 756 61, Uppsala, Sweden.
Sci Rep. 2023 Jan 31;13(1):985. doi: 10.1038/s41598-023-28147-5.
The deposition of proteins in the form of amyloid fibrils is closely associated with several serious diseases. The events that trigger the conversion from soluble functional proteins into insoluble amyloid are not fully understood. Many proteins that are not associated with disease can form amyloid with similar structural characteristics as the disease-associated fibrils, which highlights the potential risk of cross-seeding of disease amyloid by amyloid-like structures encountered in our surrounding. Of particular interest are common food proteins that can be transformed into amyloid under conditions similar to cooking. We here investigate cross-seeding of amyloid-β (Aβ), a peptide known to form amyloid during the development of Alzheimer's disease, by 16 types of amyloid fibrils derived from food proteins or peptides. Kinetic studies using thioflavin T fluorescence as output show that none of the investigated protein fibrils accelerates the aggregation of Aβ. In at least two cases (hen egg lysozyme and oat protein isolate) we observe retardation of the aggregation, which appears to originate from interactions between the food protein seeds and Aβ in aggregated form. The results support the view that food-derived amyloid is not a risk factor for development of Aβ pathology and Alzheimer's disease.
蛋白质以淀粉样纤维的形式沉积与几种严重疾病密切相关。触发可溶性功能蛋白转化为不溶性淀粉样蛋白的事件尚未完全阐明。许多与疾病无关的蛋白质可以形成与疾病相关纤维具有相似结构特征的淀粉样蛋白，这突出了在我们周围环境中遇到的淀粉样样结构对疾病淀粉样蛋白交叉接种的潜在风险。特别引人关注的是常见的食物蛋白，它们在类似于烹饪的条件下可以转化为淀粉样蛋白。在这里，我们研究了 16 种源自食物蛋白或肽的淀粉样纤维对淀粉样β（Aβ）的交叉接种，Aβ是一种在阿尔茨海默病发展过程中形成淀粉样蛋白的肽。使用硫黄素 T 荧光作为输出的动力学研究表明，所研究的任何一种蛋白纤维都不会加速 Aβ的聚集。在至少两种情况下（鸡卵溶菌酶和燕麦蛋白分离物），我们观察到聚集的延迟，这似乎源自食物蛋白种子与聚集形式的 Aβ之间的相互作用。研究结果支持这样一种观点，即源自食物的淀粉样蛋白不是 Aβ 病理和阿尔茨海默病发展的危险因素。
