کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8332142 | 1540246 | 2015 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Attenuation of lysozyme amyloid cytotoxicity by SPION-mediated modulation of amyloid aggregation
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 74, March 2015, Pages 439-446
Journal: International Journal of Biological Macromolecules - Volume 74, March 2015, Pages 439-446
نویسندگان
Aafreen Naik, Priyanka Kambli, Mohanish Borana, Neha Mohanpuria, Basir Ahmad, Varsha Kelkar-Mane, Uma Ladiwala,