Exploring the inhibitory activity of short-chain phospholipids against amyloid fibrillogenesis of hen egg-white lysozyme
| Autor: | Keng-Chi Lin, Ying-Tz Hung, Steven S.-S. Wang, Geng-Yuan Chen, Wen-Sing Wen |
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| Rok vydání: | 2010 |
| Předmět: |
Models
Molecular Amyloid Protein Denaturation Phospholipid Molecular Dynamics Simulation Fibril Protein Structure Secondary chemistry.chemical_compound Animals Humans Urea Particle Size Molecular Biology Muramidase Phospholipids chemistry.chemical_classification Chemistry Fibrillogenesis Cell Biology In vitro Enzyme Biochemistry Phosphatidylcholines Female Lysozyme Chickens |
| Zdroj: | Biochimica et biophysica acta. 1811(5) |
| ISSN: | 0006-3002 |
| Popis: | Amyloid fibrillogenesis is an important pathological feature of a group of degenerative human diseases. The 129-residue enzyme hen egg-white lysozyme has been shown to form fibrils in vitro at pH 2.0 and 55°C. In this research, using various spectroscopic techniques, light scattering, and transmission electron microscopy, we first examined the influence of short-chain phospholipids on the amyloid fibrillogenesis and the structural changes derived from hen lysozyme in vitro. Both model short-chain phospholipids were observed to mitigate the fibrillogenesis of hen lysozyme. Also, urea-induced unfolding results suggested that the susceptibility of hen lysozyme to conformational changes elicited by the denaturant was observed to decrease upon addition of short-chain phospholipids. Moreover, our molecular dynamics simulations results demonstrated that the observed inhibitory action of short-chain phosoholipids against hen lysozyme fibrillogenesis might be attributable to the interference of β-strand extension by the binding of phospholipids to lysozyme's β-sheet-rich region. We believe that the outcome from this study may contribute to a better understanding the molecular factors affecting amyloid fibrillogenesis and the molecular mechanism(s) of the interactions between phospholipids/lipids and amyloid-forming proteins. |
| Databáze: | OpenAIRE |
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