Different conformational states of hen egg white lysozyme formed by exposure to the surfactant of sodium dodecyl benzenesulfonate
| Autor: | Mukhtar Ahmed, Priyankar Sen, Anwar Ahmed, MI Khan, Salman Alamery, Hani Choudhry, Javed Masood Khan, Ajamaluddin Malik, Hajar Ahmed Almaharfi |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Amyloid
Protein Conformation Sodium Kinetics chemistry.chemical_element 02 engineering and technology Biochemistry Protein Aggregates Surface-Active Agents 03 medical and health sciences chemistry.chemical_compound Pulmonary surfactant Structural Biology Phase (matter) Molecular Biology 030304 developmental biology 0303 health sciences Spectrum Analysis Ligand binding assay Benzenesulfonates Fibrillogenesis General Medicine Hydrogen-Ion Concentration 021001 nanoscience & nanotechnology Monomer chemistry Muramidase Lysozyme 0210 nano-technology Nuclear chemistry |
| Zdroj: | International Journal of Biological Macromolecules. 128:54-60 |
| ISSN: | 0141-8130 |
| Popis: | The aim of this study was to investigate the effects of sodium dodecyl benzenesulfonate (SDBS) on hen egg white lysozyme (HEWL) fibrillogenesis at pH 7.4. HEWL fibrillogenesis in the presence of SDBS was characterized using several spectroscopic techniques (turbidity, light scattering, intrinsic fluorescence, ThT binding assay, ThT kinetics, far-UV CD, and transmission electron mmicroscopy). The turbidity and light scattering data revealed that SDBS induces aggregation in HEWL in dose-dependent manner. HEWL aggregation was seen at low SDBS concentrations (0.03 to 0.5 mM) but it was not observed at concentrations of SDBS at >0.6 mM. The ThT and TEM data clearly showed that the aggregates formed in the presence of SDBS had an amyloid-like morphology. From the CD analysis it was clear that low SDBS concentrations decreases the α-helical content while the β-sheet content increased. As the SDBS concentration further increased, the α-helical content increased again. The ThT kinetics analysis revealed that the HEWL monomer directly converted into the amyloid fibril without lag phase. All the spectroscopic and microscopic results support the finding that low concentrations of SDBS stimulate fibrillogenesis in HEWL, and that no fibrillogenesis occurs at higher SDBS concentrations. |
| Databáze: | OpenAIRE |
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