A study on the encapsulation of an occludin lipophilic derivative in liposomal carriers.
Many peptides and proteins, although potentially useful for the treatment of various diseases, are hindered in their clinical use by poor oral absorption and rapid enzymatic degradation. One of the available solutions to these problems is to increase the lipophilicity by conjugating the peptides to lipophilic moieties, making them more able to cross the biomembranes by passive transport. Occludin is a 65-kDa integral plasma-membrane protein located at the tight junctions. This protein and the peptide derived from it have potential clinical application for drug delivery. Peptide OP90-103 (1) is a fragment of occludin that shows a very poor oral bioavailability and is highly susceptible to enzymatic degradation. The conjugation of 1 with two lipoamino acid (LAA) moieties has been shown to enhance its lipophilicity and bioavailability, as well as its enzymatic stability. The purpose of this study was to evaluate the possibility of encapsulating fluorescein modified lipidated OP90-103 (2), in unilamellar- (LUV) and multilamellar liposomes (MLV), which have a different composition and surface charge and are produced by different methods. The cell internalization of the carrier systems was evaluated in vitro.
['Cupri|Sarha|S|', 'Graziano|Adriana C E|AC|', 'Cardile|Venera|V|', 'Skwarczynski|Mariusz|M|', 'Toth|Istvan|I|', 'Pignatello|Rosario|R|']
D018938:Caco-2 Cells D002470:Cell Survival D004337:Drug Carriers D016503:Drug Delivery Systems D006801:Humans D057927:Hydrophobic and Hydrophilic Interactions D008081:Liposomes D015394:Molecular Structure D062793:Occludin D010455:Peptides D014407:Tumor Cells, Cultured
lipophilicity peptides lipoamino acids fluorescein LUV Cell uptake REV fluorescence microscopy