Makshakova Olga, Bogdanova Liliya, Faizullin Dzhigangir, Khaibrakhmanova Diliara, Ziganshina Sufia, Ermakova Elena, Zuev Yuriy, Sedov Igor
Kazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center of RAS, 420111 Kazan, Russia.
Chemical Institute, Kazan Federal University, 420111 Kazan, Russia.
Pharmaceutics. 2023 Feb 13;15(2):624. doi: 10.3390/pharmaceutics15020624.
The deposition of proteins in the form of insoluble amyloid fibril aggregates is linked to a range of diseases. The supramolecular architecture of such deposits is governed by the propagation of β-strands in the direction of protofilament growth. In the present study, we analyze the structural changes of hen egg-white lysozyme fibrils upon their interactions with a range of polysaccharides, using AFM and FTIR spectroscopy. Linear anionic polysaccharides, such as κ-carrageenan and sodium alginate, are shown to be capable to disaggregate protofilaments with eventual protein renaturation. The results help to understand the mechanism of amyloid disaggregation and create a platform for both the development of new therapeutic agents for amyloidose treatment, and the design of novel functional protein-polysaccharide complex-based nanomaterials.
蛋白质以不溶性淀粉样原纤维聚集体的形式沉积与一系列疾病有关。此类沉积物的超分子结构由β-链在原纤维生长方向上的传播所决定。在本研究中，我们使用原子力显微镜（AFM）和傅里叶变换红外光谱（FTIR）分析了鸡蛋清溶菌酶原纤维与一系列多糖相互作用时的结构变化。线性阴离子多糖，如κ-卡拉胶和海藻酸钠，被证明能够分解原纤维并最终使蛋白质复性。这些结果有助于理解淀粉样蛋白解聚的机制，并为开发用于治疗淀粉样变性的新型治疗剂以及设计基于新型功能性蛋白质-多糖复合物的纳米材料创造一个平台。
