Recovery Effects of Trehalose on Acid Denaturation/Aggregation of Proteins

被引:1
|
作者
Ajito, Satoshi [1 ]
Hirai, Mitsuhiro [1 ]
机构
[1] Gunma Univ, Grad Sch Sci & Technol, 4-2 Aramaki, Maebashi, Gunma 3718510, Japan
基金
日本学术振兴会;
关键词
protein; refolding; denaturation; trehalose; X-ray scattering; X-RAY; HYDRATION; STABILIZATION; SCATTERING; MECHANISM; GLYCEROL; SUGARS;
D O I
10.2116/bunsekikagaku.68.43
中图分类号
O65 [分析化学];
学科分类号
070302 ; 081704 ;
摘要
Osmolytes, including sugars and polyols, are well known to suppress denaturation and aggregation of proteins and prevent deactivation of enzymes. Trehalose, a nonreducing disaccharide, is thought to have an excellent stabilizing action. Trehalose is produced by organisms with tolerance to extreme environments. By using synchrotron radiation X-ray wide-angle scattering (WAXS), we have found that trehalose dissociates aggregates of bovine myoglobin denatured by acidic solvents, and then folds it into a native structure. Denaturants and surfactants have been used as additives that dissociate aggregates; however, most of them are cytotoxic. Therefore, this report would suggest that trehalose is a promising candidate as a protein aggregation dissociator that is harmless to the human body. In addition, this study shows the usefulness of the wide-angle scattering method for protein structure analysis in the presence of co-solute.
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页码:43 / 49
页数:7
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