| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1987426 | International Journal of Biological Macromolecules | 2009 | 9 Pages |
Abstract
This study examined the effects of glutathione on the fibrillation of hen egg-white lysozyme. We found that the fibrillation of lysozyme was considerably reduced by GSH while no anti-aggregating activity was detected with only GSSG. SDS-PAGE results also revealed that the addition of GSH led to an early occurrence of prominent lysozyme hydrolysis. Moreover, GSH was effective in inhibiting lysozyme fibrillation when GSH was added within 6 days of incubation. We conclude that the attenuation of lysozyme fibrillation is strongly dependent upon the redox environment. Our data may contribute to decipher the molecular mechanism of amyloid fibrillation.
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Authors
Steven S.-S. Wang, Shang-Wei Chou, Kuan-Nan Liu, Chia-Hung Wu,