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• W1502016733 abstract "A new strategy for the skin delivery of bioactive compounds has been developed, using enzymes involved in the maintenance of the epidermal barrier function and the enzymatic transformation of corresponding precursors. This new strategy has been tested with regard to two enzymatic activities of the skin barrier: extracellular glucosidase and esterase/lipase. An analysis of the requirements for the glycosidic bond hydrolysis of any glycoconjugate by beta-glucocerebrosidase indicates that the release of the moiety linked to the glucose unit is obtained as long as the glycosidic bond being broken is not hindered, and as long as the leaving group property of the released moiety is good enough. This strategy was first applied to the release of the antioxidant delta-tocopherol. It was then extended to retinoic acid by introducing a spacer between the glucose unit and the bioactive moiety. This spacer was either a good leaving group such as hydroquinone, or a structure akin to a ceramide, namely glycerol. In these conditions, beta-glucocerebrosidase releases the complex spacer-active compound that is cleaved by an esterase. One of the advantages of this strategy lies in the slow release of the bioactive compound, extending in time its effect and most likely its tolerance, as is the case for retinoic acid." @default.
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• W1502016733 date "2005-08-01" @default.
• W1502016733 modified "2023-10-18" @default.
• W1502016733 title "Slow Internal Release of Bioactive Compounds Under the Effect of Skin Enzymes" @default.
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• W1502016733 doi "https://doi.org/10.1111/j.0022-202x.2005.23785.x" @default.
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