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Arylsulfatase A bound to poly(butyl cyanoacrylate) nanoparticles for enzyme replacement therapy--physicochemical evaluation.Mühlstein A, Gelperina S, Shipulo E, Maksimenko O, Kreuter J.Pharmazie. 2014 Jul;69(7):518-24статья Исследовательская статья
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: 1 апреля 2020 г.
- Авторы: Mühlstein A., Gelperina S., Shipulo E., Maksimenko O., Kreuter J.
- Журнал: Die Pharmazie
- Том: 69
- Номер: 7
- Год издания: 2014
- Издательство: Govi Verlag Pharmazeutischer Verlag GmbH
- Местоположение издательства: Germany
- Первая страница: 518
- Последняя страница: 524
- Аннотация: Arylsulfatase A (ASA) deficiency is the cause of metachromatic leucodystrophy (MLD), a lysosomal storage disease associated with severe neurological disorders. Poly(butyl cyanoacrylate) (PBCA) nanoparticles overcoated with polysorbate 80 enabled the delivery of several drugs across the blood-brain barrier to the brain suggesting that these nanoparticles also may transport ASA across this barrier. The objective of this research, therefore, was to evaluate the feasibility of loading ASA onto PBCA nanoparticles. A stable ASA-loaded PBCA nanoparticle formulation was developed that could be easily freeze-dried and stored over a period of more than 8 weeks. The maximum loading capacity for this enzyme was -59 microg per 1 mg of PBCA. In the presence of 3% sucrose as a lyoprotector the activity of freeze-dried ASA was found to be 100% recoverable.
- Добавил в систему: Гельперина Светлана Эммануиловна