Mechanical Insight into Resistance of Betaine to Urea-Induced Protein Denaturation

被引:12
作者
Chen, Jiantao [1 ]
Gong, Xiangjun [1 ]
Zeng, Chaoxi [2 ]
Wang, Yonghua [2 ]
Zhang, Guangzhao [1 ]
机构
[1] South China Univ Technol, Fac Mat Sci & Engn, Guangzhou 510640, Guangdong, Peoples R China
[2] South China Univ Technol, Coll Light Ind & Food Sci, Guangzhou 510640, Guangdong, Peoples R China
基金
中国国家自然科学基金;
关键词
NUCLEAR-MAGNETIC-RESONANCE; MOLECULAR-DYNAMICS SIMULATION; TRIMETHYLAMINE N-OXIDE; GLYCINE BETAINE; GUANIDINE-HYDROCHLORIDE; AQUEOUS-SOLUTIONS; ALPHA-CHYMOTRYPSIN; STRUCTURE BREAKER; WATER; BEHAVIOR;
D O I
10.1021/acs.jpcb.6b10172
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
It is known that urea can induce protein denaturation that can be inhibited by osmolytes. Yet, experimental explorations on this mechanism at the molecular level are still lacking. We have investigated the resistance of betaine to the urea-induced denaturation of lysozyme in aqueous solutions using low-field NMR. Our study demonstrates that urea molecules directly interact with lysozyme, leading to denaturation. However, betaine molecules interacting with urea more strongly than lysozyme can pull the bound urea molecules from lysozyme so that the protein is protected from denaturation. The number of urea molecules bound to a betaine molecule is given under different conditions. Proton NMR spectroscopy (H-1-NMR) and Fourier transform infrared spectroscopy reveal that the interaction between betaine and urea is through hydrogen bonding.
引用
收藏
页码:12327 / 12333
页数:7
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