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Combined action of chemical chaperones on stability, aggregation and oligomeric state of muscle glycogen phosphorylase bстатья
Статья опубликована в высокорейтинговом журнале
Статья опубликована в журнале из списка Web of Science и/или Scopus- Авторы: Eronina Tatiana B., Mikhaylova Valeriya V., Chebotareva Natalia A., Kleymenov Sergey Y., Pivovarova Anastasia V., Kurganov Boris I.
- Журнал: International Journal of Biological Macromolecules
- Том: 203
- Год издания: 2022
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 406
- Последняя страница: 416
- DOI: 10.1016/j.ijbiomac.2022.01.106
- Аннотация: Chemical chaperones are a class of small molecules, which enhance protein stability, folding, inhibit protein aggregation, and are used for long-term storage of therapeutic proteins. The combined action of chemical chaperones trehalose, betaine and lysine on stability, aggregation and oligomeric state of muscle glycogen phosphorylase b (Phb) has been studied. Dynamic light scattering data indicate that the affinity of trehalose to Phb increased in the presence of betaine or lysine at both stages (stage of nucleation and aggregate growth) of enzyme aggregation at 48 °C, in contrast, the affinity of betaine to the enzyme in the presence of lysine remained practically unchanged. According to differential scanning calorimetry and analytical ultracentrifugation data, the mixture of trehalose and betaine stabilized Phb stronger than either of them in total. Moreover, the destabilizing effect of lysine on the enzyme was almost completely compensated by trehalose and only partially by betaine. The main protective effect of the mixtures of osmolytes and lysine is associated with their influence on the dissociation/denaturation stage, which is the rate-limiting one of Phb aggregation. Thus, a pair of chaperones affects the stability, oligomeric state, and aggregation of Phb differently than individual chaperones.
- Добавил в систему: Фурсова Полина Викторовна