AIE-Based Dynamic in Situ Nanoscale Visualization of Amyloid Fibrillation from Hen Egg White Lysozyme
| Autor: | Cheng Fan, Ya-Long Wang, Ming-Qiang Zhu, Yu-Xuan Su, Peng-Ju Zhao, Chong Li, Hong-Qing Qu |
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| Rok vydání: | 2020 |
| Předmět: |
Pharmacology
Fibrillation 010405 organic chemistry Chemistry Organic Chemistry Biomedical Engineering Beta sheet Pharmaceutical Science Bioengineering 02 engineering and technology Protein aggregation 021001 nanoscience & nanotechnology 01 natural sciences Fluorescence 0104 chemical sciences chemistry.chemical_compound Protein structure Fluorescence microscope Biophysics medicine Protein folding Lysozyme medicine.symptom 0210 nano-technology Biotechnology |
| Zdroj: | Bioconjugate Chemistry. 31:2303-2311 |
| ISSN: | 1520-4812 1043-1802 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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