The Effect of Arginine on the Phase Stability of Aqueous Hen Egg-White Lysozyme Solutions

被引:4
|
作者
Brudar, Sandi [1 ]
Hribar-Lee, Barbara [1 ]
机构
[1] Univ Ljubljana, Fac Chem & Chem Technol, Vecna Pot 113, SI-1000 Ljubljana, Slovenia
基金
美国国家卫生研究院;
关键词
hen egg-white lysozyme; arginine; cloud-point temperature; molecular dynamics; self-association; phase stability of protein solutions; force field effect; PROTEIN AGGREGATION; FORCE-FIELDS; SEPARATION; MECHANISM;
D O I
10.3390/ijms24021197
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The effect of arginine on the phase stability of the hen egg-white lysozyme (HEWL) has been studied via molecular dynamics computer simulations, as well as experimentally via cloud-point temperature determination. The experiments show that the addition of arginine increases the stability of the HEWL solutions. The computer simulation results indicate that arginine molecules tend to self-associate. If arginine residues are located on the protein surface, the free arginine molecules stay in their vicinity and prevent the way protein molecules "connect" through them to form clusters. The results are not sensitive to a particular force field and suggest a possible microscopic mechanism of the stabilizing role of arginine as an excipient.
引用
收藏
页数:11
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