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Effect of membranotropic and mucoadhesive formulations of protein proteinase inhibitors on bovine herpes virus-1 reproductionстатья
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 26 ноября 2014 г.
- Авторы: Larionova N.V., Malykh E.V., Villemson A.L., Krasota A.Ju, Duchene D., Ollivon M., Gernet M.V., Belousova R.V., Shen W-C, Larionova N.I.
- Журнал: International Journal of Pharmaceutics
- Том: 256
- Номер: 1-2
- Год издания: 2003
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 191
- Последняя страница: 198
- DOI: 10.1016/S0378-5173(03)00077-2
- Аннотация: The lipidized derivatives of Bowman-Birk soybean protease inhibitor (BBI) containing one to three oleoyl groups were synthesized and characterized. The (ole)(1)- and (ole)(2)BBI were demonstrated to have 200- and 100-fold higher uptake into Caco-2 cell monolayers compared to native BBI. The acylated BBI had increased affinity to elastase-like proteases. Aprotinin-loaded starch/bovine serum albumin microcapsules were prepared using interfacial cross-linking with terephthaloyl chloride and characterized for their morphology, size and release of the inhibitor. Various formulations of protein proteinase inhibitors were tested for their influence on BHV-1 reproduction in cell cultures. Native aprotinin possessed palpable dose-dependent effect inhibiting the virus reproduction up to 4.0 lg (10,000-fold). The bioadhesive, biodegradable aprotinin-loaded microcapsules were the most effective decreasing virus infectious titer up to 4.0 lg and delaying the cytopathic effect up to 144 h in lesser doses of aprotinin. The lipophilic derivative (ole)(1)BBI was shown to exhibit effective inhibition (>100-fold) of BHV-1 reproduction unlike native BBI.
- Добавил в систему: Красота Александр Юрьевич