title: A study on the encapsulation of an occludin lipophilic derivative in liposomal carriers.
abstract: 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.
authors.affiliation: a Section of Pharmaceutical Technology, Department of Drug Sciences , University of Catania , Catania , Italy .
authors.forename: Sarha
authors.initials: S
authors.lastname: Cupri
authors.affiliation: b Section of Physiology, Department of Bio-medical Sciences , University of Catania , Catania , Italy .
authors.forename: Adriana C E
authors.initials: AC
authors.lastname: Graziano
authors.affiliation: b Section of Physiology, Department of Bio-medical Sciences , University of Catania , Catania , Italy .
authors.forename: Venera
authors.initials: V
authors.lastname: Cardile
authors.affiliation: c School of Chemistry and Molecular Biosciences, The University of Queensland , Brisbane , Queensland , Australia , and.
authors.forename: Mariusz
authors.initials: M
authors.lastname: Skwarczynski
authors.affiliation: c School of Chemistry and Molecular Biosciences, The University of Queensland , Brisbane , Queensland , Australia , and.|d School of Pharmacy, The University of Queensland , Brisbane , Queensland , Australia.
authors.forename: Istvan
authors.initials: I
authors.lastname: Toth
authors.affiliation: a Section of Pharmaceutical Technology, Department of Drug Sciences , University of Catania , Catania , Italy .
authors.forename: Rosario
authors.initials: R
authors.lastname: Pignatello
mesh_terms: D018938:Caco-2 Cells; D002470:Cell Survival / Q000187:drug effects; D004337:Drug Carriers / Q000737:chemistry*; D016503:Drug Delivery Systems; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008081:Liposomes; D015394:Molecular Structure; D062793:Occludin / Q000138:chemical synthesis / Q000737:chemistry*; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry; D014407:Tumor Cells, Cultured
chemical_list: D004337:Drug Carriers; D008081:Liposomes; D062793:Occludin; D010455:Peptides
keywords: Cell uptake; LUV; REV; fluorescein; fluorescence microscopy; lipoamino acids; lipophilicity; peptides