Biophysical effect of amino acids on the prevention of protein aggregation
Biophysical effect of amino acids on the prevention of protein aggregation
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DOI：
10.1093/oxfordjournals.jbchem.a003261
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发表时间：
2002-10-01
影响因子：
2.7
通讯作者：
Takagi, M
中科院分区：
文献类型：
--
作者：
Shiraki, K;Kudou, M;Takagi, M
每种蛋白质都会自发折叠成独特的天然结构。然而，在解折叠或重折叠过程中，蛋白质往往倾向于形成聚集体。为了建立一种方法，以防止不希望的蛋白质聚集，并增加在恶化条件下的天然蛋白质结构的稳定性，两种类型的聚集条件，热展开诱导的聚集和稀释诱导的聚集从变性状态，在存在额外的氨基酸和离子使用溶菌酶作为模型蛋白质。在测试的15种氨基酸中，精氨酸在两种情况下都表现出防止聚集体形成的最佳结果。进一步的生物物理研究表明，精氨酸并没有改变溶菌酶的热变性温度（Tm）。精氨酸对聚集的抑制作用不依赖于8种蛋白质的大小或等电点。
Each protein folds into a unique and native structure spontaneously. However, during the unfolding or refolding process, a protein often tends to form aggregates. To establish a method to prevent undesirable protein aggregation and to increase the stability of native protein structures under deterioration conditions, two types of aggregation conditions, thermal unfolding-induced aggregation and dilution-induced aggregation from denatured state, were studied in the presence of additional amino acids and ions using lysozyme as a model protein. Among 15 amino acids tested, arginine exhibited the best results in preventing the formation of aggregates in both cases. Further biophysical studies revealed that arginine did not change the thermal denaturation temperature (T-m) of the lysozyme. The preventive effect of arginine on aggregation was not dependent on the size or isoelectric point of eight kinds of proteins tested.