Attenuation of lysozyme amyloid cytotoxicity by SPION-mediated modulation of amyloid aggregation
| Autor: | Priyanka Kambli, Basir Ahmad, Uma Ladiwala, Varsha Kelkar-Mane, Neha Mohanpuria, Mohanish Borana, Aafreen Naik |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
Amyloid
Biochemistry Cell Line Mice Protein Aggregates chemistry.chemical_compound Structural Biology mental disorders Animals Humans Cytotoxic T cell Magnetite Nanoparticles Cytotoxicity Molecular Biology Chemistry P3 peptide General Medicine Kinetics Toxicity Amyloid aggregation Biophysics Muramidase Lysozyme Iron oxide nanoparticles |
| Zdroj: | International Journal of Biological Macromolecules. 74:439-446 |
| ISSN: | 0141-8130 |
| DOI: | 10.1016/j.ijbiomac.2014.12.040 |
| Popis: | The formation and deposition of proteinaceous aggregates of amyloid fibrils characterize diverse degenerative diseases, such as Alzheimer's, Parkinson's, and systemic amyloidosis. The presence of these aggregates is associated with clinical manifestations, and various forms of amyloid aggregates have been identified to be cytotoxic. Although the exact mechanism of amyloid toxicity remains to be elucidated, prevention of amyloid fibril formation and aggregation forms a possible therapeutic approach. Nanomaterials possess the potential for such a strategy. Using hen egg white lysozyme (HEWL) as a prototypic amyloid-forming protein, we found a reduction in the aggregation rate of HEWL in the presence of super-paramagnetic iron oxide nanoparticles (SPIONs) with slowing of nucleation and amyloid fibril elongation. HEWL-amyloid had a predominantly fibrillar structure and was toxic to various cells. A significant attenuation of cytotoxicity was observed when cells were treated with SPION-interacted HEWL-amyloid. Ultra-structural differences were observed between the native and SPION-interacted HEWL-amyloids by SEM and TEM imaging. Our findings confirm that SPIONs perturb amyloid fibrillation, thereby reducing the cytotoxicity of amyloid. |
| Databáze: | OpenAIRE |
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