https://scholars.lib.ntu.edu.tw/handle/123456789/406745
標題: | Effects of dithiothreitol on the amyloid fibrillogenesis of hen egg-white lysozyme | 作者: | Wang S.S.-S. Liu K.-N. Wang B.-W. |
關鍵字: | Amyloid fibril;Disulfide bond;Dithiothreitol;Inhibition;Lysozyme;Reductant | 公開日期: | 2010 | 卷: | 39 | 期: | 8 | 起(迄)頁: | 1229-1242 | 來源出版物: | European Biophysics Journal | 摘要: | At least 25 human proteins can fold abnormally to form pathological deposits that are associated with several degenerative diseases. Despite extensive investigation on amyloid fibrillation, the detailed molecular mechanisms remain rather elusive and there are currently no effective cures for treating these amyloid diseases. The present study examined the effects of dithiothreitol on the fibrillation of hen egg-white lysozyme (HEWL). Our results revealed that the fibrillation of hen lysozyme was significantly inhibited by reduced dithiothreitol (DTTred) while oxidized dithiothreitol (DTTox) had no anti-aggregating activity. Effective inhibitory activity against hen lysozyme fibrillation was observed only when DTT red was added within 8 days of incubation. Our results showed that the initial addition of DTTred interacted with HEWL, leading to a loss in conformational stability. It was concluded from our findings that DTTred-induced attenuation of HEWL fibrillation may be associated with disulfide disruption and extensive structural unfolding of HEWL. Our data may contribute to rational design of effective therapeutic strategies for amyloid diseases. ? 2010 European Biophysical Societies' Association. |
URI: | https://scholars.lib.ntu.edu.tw/handle/123456789/406745 | ISSN: | 01757571 | DOI: | 10.1007/s00249-010-0576-0 | SDG/關鍵字: | amyloid; avian protein; central nervous system agents; dithiothreitol; egg protein; egg white; lysozyme; urea; amyloid; avian protein; central nervous system agents; dithiothreitol; egg protein; lysozyme; animal; article; chemistry; chicken; drug effect; female; hydrophobicity; kinetics; metabolism; oxidation reduction reaction; protein conformation; protein folding; protein multimerization; protein stability; thermodynamics; chemical phenomena; drug effects; metabolism; protein multimerization; Amyloid; Animals; Avian Proteins; Central Nervous System Agents; Chickens; Dithiothreitol; Egg Proteins; Egg White; Female; Hydrophobicity; Kinetics; Muramidase; Oxidation-Reduction; Protein Conformation; Protein Folding; Protein Multimerization; Protein Stability; Thermodynamics; Urea; Amyloid; Animals; Avian Proteins; Central Nervous System Agents; Chickens; Dithiothreitol; Egg Proteins; Egg White; Female; Hydrophobic and Hydrophilic Interactions; Kinetics; Muramidase; Oxidation-Reduction; Protein Conformation; Protein Folding; Protein Multimerization; Protein Stability; Thermodynamics; Urea |
顯示於: | 化學工程學系 |
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