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Peptide-protein complex from cattle sclera: Structural aspects and chaperone activityстатья
- Авторы: Ilyina A.P., Sidorsky E.V., Tregubov A.V., Chekova V.M., Elistratov P.A., Yamskova V.P., Yamskov I.A.
- Журнал: Biochemistry and Biophysics Reports
- Номер: 24
- Год издания: 2020
- Первая страница: 1
- Последняя страница: 10
- Номер статьи: 1-10
- DOI: 10.1016/j.bbrep.2020.100851
- Аннотация: The influence of temperature and chaotropic agents on the spatial organization of the peptide-protein complex isolated from cattle sclera at the level of secondary structure was studied by UV, CD spectroscopy, and dynamic light scattering. It is shown that this complex has high conformational thermostability. The point of confor- mational thermal transition (65 ◦C) was determined, after which the peptide-protein complex passes into a denatured stable state. It was found that the peptide-protein complex in aqueous solutions forms thermostable nanosized particles. It was shown that the peptide-protein complex isolated from cattle sclera shows the prop- erties of chaperone, an inhibitor of model protein aggregation induced by dithiothreitol.
- Добавил в систему: Сидорский Егор Владимирович