Federal State Institution "Federal Research Centre "Fundamentals of Biotechnology" of the Russian Academy of Sciences", Leninsky pr. 33, Moscow, 119071, Russia.
Kol'tsov Institute of Developmental Biology, Russian Academy of Sciences, 26 Vavilova str, Moscow, 119991, Russia.
Sci Rep. 2017 Jun 21;7(1):3984. doi: 10.1038/s41598-017-04409-x.
Chemical chaperones including arginine and its derivatives are widely used by biochemists working on the design of agents, which are able to efficiently suppress protein aggregation. To elucidate the mechanisms of anti-aggregation activity of chemical chaperones, methods based on registration of the increment in light scattering intensity must be supplemented with methods for direct detection of the portion of aggregated protein (γ). For this purpose asymmetric flow field-flow fractionation was used in the present work. It was shown that heat-induced aggregation of bovine serum albumin (BSA) followed the kinetics of the reaction of the second order (0.1 M sodium phosphate buffer, pH 7.0, 70 °C). It was proposed to use R vs γ plots to characterize the aggregation pathway (R is the hydrodynamic radius of the protein aggregates, which was calculated from the dynamic light scattering data). The changes in the shape of R vs γ plots in the presence of arginine, arginine amide and arginine ethyl ester are indicative of the changes in the aggregation pathway of BSA aggregation. A conclusion has been made that larger aggregates are formed in the presence of arginine hydrochloride and its derivatives.
化学伴侣包括精氨酸及其衍生物，被从事设计能够有效抑制蛋白质聚集的试剂的生化学家广泛使用。为了阐明化学伴侣的抗聚集活性的机制，必须用直接检测聚集蛋白（γ）部分的方法来补充基于光散射强度增量的登记方法。为此，本工作中使用了不对称流场流分离。结果表明，牛血清白蛋白（BSA）的热诱导聚集遵循二级反应动力学（0.1 M 磷酸钠缓冲液，pH 7.0，70°C）。有人建议使用 R 与γ的关系图来描述聚集途径（R 是蛋白质聚集体的流体力学半径，它是根据动态光散射数据计算出来的）。在精氨酸、精氨酸酰胺和精氨酸乙酯存在下，R 与γ关系图的形状变化表明 BSA 聚集的聚集途径发生了变化。得出的结论是，在盐酸精氨酸及其衍生物的存在下形成了更大的聚集体。
