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EnglishCelecoxib (CLX) delivery and its enzyme-sensitive release from Inulin-d-alfa-tocopherol succinate (INVITE) nanomicelles are the main goals of this paper. CLX is a highly hydrophobic drug belonging to BCS class II (low solubility, high permeability). For this reason its formulation is problematic and its biopharmaceutical performances strongly depend from the applied delivery system. In the last years INVITE nanomicelles shown their potential in the delivery of highly hydrophobic drugs such as curcumin and for this reason have been chosen as a good candidate for CLX delivery. Furthermore, due to the presence of ester bonds between INU and VITE it has been supposed that the drug release could show enzyme-sensitive (esterase) behaviors. Thus CLX was loaded in INVITE nanomicelles, the loading was quantified and the physical stability was evaluated till 90 days, finally, drug release studies in the presence or not of the specific enzyme esterase were performed.
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| Titolo: | Enzyme controlled release of celecoxib from inulin based nanomicelles |
| Autori: | |
| Data di pubblicazione: | 2015 |
| Rivista: | |
| Abstract: | Celecoxib (CLX) delivery and its enzyme-sensitive release from Inulin-d-alfa-tocopherol succinate (INVITE) nanomicelles are the main goals of this paper. CLX is a highly hydrophobic drug belonging to BCS class II (low solubility, high permeability). For this reason its formulation is problematic and its biopharmaceutical performances strongly depend from the applied delivery system. In the last years INVITE nanomicelles shown their potential in the delivery of highly hydrophobic drugs such as curcumin and for this reason have been chosen as a good candidate for CLX delivery. Furthermore, due to the presence of ester bonds between INU and VITE it has been supposed that the drug release could show enzyme-sensitive (esterase) behaviors. Thus CLX was loaded in INVITE nanomicelles, the loading was quantified and the physical stability was evaluated till 90 days, finally, drug release studies in the presence or not of the specific enzyme esterase were performed. |
| Handle: | http://hdl.handle.net/11571/1088387 |
| Appare nelle tipologie: | 1.1 Articolo in rivista |
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