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Effect of Soft Preheating of Bovine Serum Albumin on the Complexation with Oligochitosan: Structure and Conformation of BSA in the Complexстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 17 апреля 2024 г.
- Авторы: Zhuravleva Irina L., Bezrodnykh Evgeniya A., Berezin Boris B., Tikhonov Vladimir E., Antonov Yurij A.
- Журнал: Macromolecular Bioscience
- Год издания: 2023
- Издательство: John Wiley & Sons Ltd.
- Местоположение издательства: United Kingdom
- Номер статьи: 2300088
- DOI: 10.1002/mabi.202300088
- Аннотация: Phase analysis, spectroscopic and light scattering methods are applied to investigate the peculiarities of the interaction of oligochitosan (OCHI) with native and preheated BSA as well as the conformational and structural changes of BSA in BSA/OCHI complex. As shown, untreated BSA binds with OCHI mainly forming soluble electrostatic nanocomplexes, with the binding causing an increase in BSA helicity without a change in the local tertiary structure and thermal stability of BSA. In contrast, soft preheating at 56oC enhances the complexation of BSA with OCHI and slightly destabilizes the secondary and local tertiary structures of BSA within the complex particles. Preheating at 64oC (below the irreversible stage of BSA thermodenaturation) leads to further enhancement in the complexation and formation of insoluble complexes stabilized by both Coulomb forces and hydrophobic interactions. The finding can be promising for the preparation of biodegradable BSA/chitosan-based drug delivery systems.
- Добавил в систему: Тихонов Владимир Евгеньевич
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