Shiraki Kentaro, Kudou Motonori, Fujiwara Shinsuke, Imanaka Tadayuki, Takagi Masahiro
School of Materials Science, Japan Advanced Institute of Science and Technology, Asahidai, Tatsunokuchi, Ishikawa 923-1292, Japan.
J Biochem. 2002 Oct;132(4):591-5. doi: 10.1093/oxfordjournals.jbchem.a003261.
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.
每种蛋白质都会自发折叠成独特的天然结构。然而，在去折叠或重折叠过程中，蛋白质往往容易形成聚集体。为了建立一种方法来防止不期望的蛋白质聚集，并在劣化条件下提高天然蛋白质结构的稳定性，以溶菌酶为模型蛋白，在存在额外氨基酸和离子的情况下，研究了两种聚集条件，即热去折叠诱导聚集和变性状态下的稀释诱导聚集。在所测试的15种氨基酸中，精氨酸在两种情况下防止聚集体形成方面都表现出最佳效果。进一步的生物物理研究表明，精氨酸不会改变溶菌酶的热变性温度（T(m)）。精氨酸对聚集的预防作用不依赖于所测试的8种蛋白质的大小或等电点。
