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Preparation and Characterization of pH-Sensitive Capsosomes for Oral Delivery of Therapeutic Proteins

DC Field Value Language
dc.contributor.authorYang, Eunhye-
dc.contributor.authorJung, Ho -Sup-
dc.contributor.authorChang, Pahn-Shick-
dc.date.accessioned2022-10-12T00:56:22Z-
dc.date.available2022-10-12T00:56:22Z-
dc.date.created2022-08-12-
dc.date.issued2022-08-
dc.identifier.citationLangmuir, Vol.38 No.30, pp.9294-9300-
dc.identifier.issn0743-7463-
dc.identifier.urihttps://hdl.handle.net/10371/185932-
dc.description.abstractOral administration of therapeutic proteins is very challenging because of gastrointestinal instability and decomposition. In this study, we developed a system for oral delivery of superoxide dismutase (SOD) as one of the therapeutic proteins. SOD-loaded capsosomes (SOD-C) were formed by the assembly of chitosan-coated solid lipid nanoparticles and SOD-loaded liposomes (SOD-L). Unlike raw SOD activity decreases to 19.41% in SGF and 13.70% in SIF, the SOD-C in SGF (89.30%) condition retained its initial catalytic activity and decreased but exhibited a three-fold higher raw SOD activity even after incubation in SIF (41.63%). TEM analysis indicated that after intestinal digestion, the residual amount of intact liposomes affected the higher catalytic activity of SOD-C compared to raw SOD and SOD-L. Based on these results, significantly higher cellular uptake of SOD-C was observed compared to raw SOD. Also, SOD-C remarkably suppressed the cellular malondialdehyde (MDA) concentration by maintaining the antioxidative capacity of SOD to remove MDA produced in the oxidative stress-induced cells, thereby contributing to a significant five-fold difference with SOD-R (p < 0.05). This delivery system can facilitate the oral application of other therapeutic proteins, improving gastrointestinal stability.-
dc.language영어-
dc.publisherAmerican Chemical Society-
dc.titlePreparation and Characterization of pH-Sensitive Capsosomes for Oral Delivery of Therapeutic Proteins-
dc.typeArticle-
dc.identifier.doi10.1021/acs.langmuir.2c01089-
dc.citation.journaltitleLangmuir-
dc.identifier.wosid000833001500001-
dc.identifier.scopusid2-s2.0-85135500880-
dc.citation.endpage9300-
dc.citation.number30-
dc.citation.startpage9294-
dc.citation.volume38-
dc.description.isOpenAccessN-
dc.contributor.affiliatedAuthorChang, Pahn-Shick-
dc.type.docTypeArticle-
dc.description.journalClass1-
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