| Autor: |
Borzova VA; Federal State Institution 'Federal Research Centre 'Fundamentals of Biotechnology' of the Russian Academy of Sciences', Leninsky pr. 33, Moscow, 119071, Russia., Markossian KA; Federal State Institution 'Federal Research Centre 'Fundamentals of Biotechnology' of the Russian Academy of Sciences', Leninsky pr. 33, Moscow, 119071, Russia., Kleymenov SY; Kol'tsov Institute of Developmental Biology, Russian Academy of Sciences, 26 Vavilova str, Moscow, 119991, Russia., Kurganov BI; Federal State Institution 'Federal Research Centre 'Fundamentals of Biotechnology' of the Russian Academy of Sciences', Leninsky pr. 33, Moscow, 119071, Russia. kurganov@inbi.ras.ru. |
| Abstrakt: |
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 agg ). 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 h vs γ agg plots to characterize the aggregation pathway (R h is the hydrodynamic radius of the protein aggregates, which was calculated from the dynamic light scattering data). The changes in the shape of R h vs γ agg 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. |
