Effects of glutathione on amyloid fibrillation of hen egg-white lysozyme.
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.
Wang
Steven S-S
SS
Department of Chemical Engineering, National Taiwan University, No. 1, Sec. 4, Roosevelt Rd., Taipei 10617, Taiwan. sswang@ntu.edu.tw
Chou
Shang-Wei
SW
Liu
Kuan-Nan
KN
Wu
Chia-Hung
CH
D000682:Amyloid / Q000378:metabolism*; D000818:Animals; D004220:Disulfides / Q000737:chemistry; D004586:Electrophoresis; D005978:Glutathione / Q000494:pharmacology*; D057927:Hydrophobic and Hydrophilic Interactions; D008854:Microscopy, Electron; D009113:Muramidase / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding / Q000187:drug effects; D017433:Protein Structure, Secondary / Q000187:drug effects; D013057:Spectrum Analysis; D013499:Surface Properties / Q000187:drug effects; D013997:Time Factors
D000682:Amyloid; D004220:Disulfides; C421864:hen egg lysozyme; D009113:Muramidase; D005978:Glutathione