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• W1994540515 abstract "Omeprazole (OME) exhibits low stability to light, heat and humidity. In stress conditions OME stability should improve under inclusion complex form with hydroxypropyl-β-cyclodextrin (HPβCD). Stability of OME, its physical mixture (PM) with HPβCD and OME:HPβCD inclusion complex was assessed during 60 days. The inclusion complexes were prepared by kneading and freeze-drying techniques and characterized by differential scanning calorimetry (DSC) and Fourier transform infrared spectroscopy (FTIR). A molecular modelling was also held to predict the most probable tridimensional conformation of inclusion complex OME:HPβCD. The inhibitory activity of free and complexed OME on selected enzymes, namely, papain (protease model of the proton pump) and acetylcholinesterase (enzyme present in cholinergic neurons and also involved in Alzheimer’s disease) was compared. The results obtained show that HPβCD do not protect against OME degradation, in any prepared powder, in the presence of light, heat and humidity. This may indicate that the reactive group of OME is not included in the HPβCD cavity. This fact is supported by molecular modelling data, which demonstrated that 2-pyridylmethyl group of OME is not included into the cyclodextrin cavity. In relation to enzymatic assays it was observed that free OME and OME in the binary systems showed identical inhibitory activity on papain and acethylcolinesterase, concluding that HPβCD do not affect OME activity on these two enzymes." @default.
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• W1994540515 date "2010-10-28" @default.
• W1994540515 modified "2023-10-18" @default.
• W1994540515 title "Stability and enzymatic studies with omeprazole:hydroxypropyl-β-cyclodextrin" @default.
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• W1994540515 doi "https://doi.org/10.1007/s10847-010-9884-3" @default.
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