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Supramolecular assemblies of mucin and lysozyme: Formation andphysicochemical characterizationстатья
- Авторы: Filatova Lyubov, Emelianov Georgii, Balabushevich Nadezhda, Klyachko Natalia
- Журнал: Process Biochemistry
- Год издания: 2021
- Издательство: Elsevier Applied Science
- Местоположение издательства: United Kingdom
- DOI: 10.1016/j.procbio.2021.12.022
- Аннотация: Mucin and lysozyme are the most important components of mucous membranes. The complexes of pig gastric mucin (PGM) and the bacteriolytic enzyme lysozyme (LZ) have been studied using a wide range of physicochemical methods (turbidimetry, light scattering, fluorescence, electron microscopy, chromatography, and electrophoresis). The strongest binding of LZ to PGM was observed at pH 6–7 in a salt–free medium. Complexes between biomolecules were formed due to electrostatic interactions between the positively charged amino groups of LZ and the negatively charged carboxyl groups of the carbohydrate shell of PGM, van der Waals forces, and hydrogen bonds. Supramolecular LZ:PGM assemblies were polydisperse heterogeneous microaggregates with both LZ and PGM molecules located on their surface. The LZ activity in the presence of PGM changed through both the formation of complexes and the fact that PGM caused an increase in the viscosity of the medium and created diffusion restrictions for the enzyme’s access to the cellular substrate. Based on the data obtained, strategies can be developed to regulate antimicrobial properties of lytic enzymes (and their complexes with mucins) for mucosal use.
- Добавил в систему: Филатова Любовь Юрьевна
Прикрепленные файлы
| № | Имя | Описание | Имя файла | Размер | Добавлен |
|---|---|---|---|---|---|
| 1. | Первая страница | Process_Biochemistry.pdf | 255,6 КБ | 14 января 2022 [FilatovaLYu] |