Celecoxib (CLX) delivery and its enzyme-sensitive release from Inulin-d-alfa-tocopherol succinate (INVITE) nanomi- celles 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 has been 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 up to 90 days, finally, drug release studies in the presence or in the absence of the specific enzyme esterase were performed.
Enzyme controlled release of celecoxib from inulin based nanomicelles
MANDRACCHIA, DELIA;
2015-01-01
Abstract
Celecoxib (CLX) delivery and its enzyme-sensitive release from Inulin-d-alfa-tocopherol succinate (INVITE) nanomi- celles 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 has been 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 up to 90 days, finally, drug release studies in the presence or in the absence of the specific enzyme esterase were performed.File | Dimensione | Formato | |
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