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AIE-Based Dynamic in Situ Nanoscale Visualization of Amyloid Fibrillation from Hen Egg White Lysozyme
Bioconjugate Chemistry ( IF 4.7 ) Pub Date : 2020-10-01 , DOI: 10.1021/acs.bioconjchem.0c00379
Cheng Fan 1 , Ya-Long Wang 2 , Peng-Ju Zhao 1, 3 , Hong-Qing Qu 1 , Yu-Xuan Su 1 , Chong Li 1 , Ming-Qiang Zhu 1, 2
Affiliation  

Protein misfolding and denaturation, represented by amyloid fibrillation, are associated with many diseases. However, as a general chemical biological process, the dynamic structure information on amyloid fibrillation has not been demonstrated categorically. Herein, hen egg white lysozyme (HEWL) was used as the model protein of interest to realize in situ nanoscale imaging of protein fibrillation process using the fluorophores with aggregation-induced emission (AIE) activity. The AIE-active fluorophores exhibit the reversible capability of association and dissociation with β-sheet structure and thus dynamic binding-induced emission, which causes the spontaneous switching of fluorescence. The entire HEWL denaturation process induced by sodium dodecyl sulfate (SDS) at ambient conditions was demonstrated in detail by using two AIE-active fluorophores (TPE-NaSO3 and PD-BZ-OH) through reversible electrostatic interaction and specific labeling between AIE probes and β-sheet structures of amyloid fibrils, respectively. The results indicate that PD-BZ-OH is more specific AIE probe for amyloid fibrils than TPE-NaSO3. In comparison, the SEM and TEM results show the same denaturation process of protein fibrillation induced by SDS at different concentrations. The static super-resolution imaging of amyloid fibrils is performed with a resolution of 35 nm using PD-BZ-OH aqueous solution without additional auxiliary conditions. The dynamic evolution process of HEWL amyloid fibrillation is in situ visualized through super-resolution fluorescent microscopy with nanoscale resolution. Both static and dynamic super-resolution imaging of amyloid fibrillation provides detailed nanoscale structure information exceeding 50 nm resolution, which is of great significance in the exploration of amyloid fibrillation and related diseases.

中文翻译:

基于AIE的鸡蛋清溶菌酶对淀粉样纤维化的动态原位纳米可视化

以淀粉样蛋白原纤化为代表的蛋白质错误折叠和变性与许多疾病有关。然而,作为一般的化学生物学过程,关于淀粉样蛋白原纤化的动态结构信息尚未得到分类证实。在此,将鸡卵清溶菌酶(HEWL)用作感兴趣的模型蛋白以原位实现纳米级成像的蛋白质原纤化过程中使用具有聚集诱导发射(AIE)活性的荧光团。AIE活性荧光团表现出与β-折叠结构可逆的缔合和解离能力,因此具有动态结合诱导发射,从而引起荧光的自发转换。通过使用两个AIE活性荧光团(TPE-NaSO 3和PD-BZ-OH),通过可逆的静电相互作用和AIE探针之间的特异性标记,详细证明了十二烷基硫酸钠(SDS)在环境条件下诱导的整个HEWL变性过程。淀粉样蛋白原纤维的β-折叠结构。结果表明,PD-BZ-OH比TPE-NaSO 3对淀粉样原纤维的特异性更强。。相比之下,SEM和TEM结果显示了不同浓度SDS诱导的蛋白原纤化的相同变性过程。使用PD-BZ-OH水溶液以35 nm的分辨率对淀粉样蛋白原纤维进行静态超分辨率成像,而无需其他辅助条件。HEWL淀粉样蛋白原纤维的动态演变过程通过具有纳米级分辨率的超分辨率荧光显微镜原位观察。淀粉样蛋白原纤化的静态和动态超分辨率成像均提供超过50 nm分辨率的详细的纳米级结构信息,这在淀粉样蛋白原纤化及相关疾病的探索中具有重要意义。
更新日期:2020-10-21
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