Please use this identifier to cite or link to this item: https://doi.org/10.1002/marc.201000176
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dc.titleTailored albumin-based copolymers for receptor-mediated delivery of perylenediimide guest molecules
dc.contributor.authorEisele, K.
dc.contributor.authorGropeanu, R.
dc.contributor.authorMusante, A.
dc.contributor.authorGlasser, G.
dc.contributor.authorLi, C.
dc.contributor.authorMuellen, K.
dc.contributor.authorWeil, T.
dc.date.accessioned2014-10-16T08:44:56Z
dc.date.available2014-10-16T08:44:56Z
dc.date.issued2010-09-01
dc.identifier.citationEisele, K., Gropeanu, R., Musante, A., Glasser, G., Li, C., Muellen, K., Weil, T. (2010-09-01). Tailored albumin-based copolymers for receptor-mediated delivery of perylenediimide guest molecules. Macromolecular Rapid Communications 31 (17) : 1501-1508. ScholarBank@NUS Repository. https://doi.org/10.1002/marc.201000176
dc.identifier.issn10221336
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/95193
dc.description.abstractFigure Presented The synthesis of a novel and multifunctional copolymer based on a human serum albumin backbone bearing several folic acid as well as PEO groups was presented. In solution, this sidechain copolymer adopts a globular architecture and about five molecules of the waterinsoluble chromophore PDI were successfully incorporated into these micelles for receptor-mediated cell uptake investigations. A significant uptake of these bioconjugates via receptor-mediated endocytosis was detected for cells expressing folic acid receptors in the cell membrane. These novel albumin-based copolymers could serve as efficient and biocompatible carrier systems facilitating the directed delivery of lipophilic drug molecules into cancer cells and they allow investigating vesicle formation and trafficking even at the single molecule level. © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1002/marc.201000176
dc.sourceScopus
dc.subjectCopolymer
dc.subjectEndocytosis
dc.subjectFolic acid
dc.subjectHuman serum albumin
dc.subjectProtein hybrid
dc.typeArticle
dc.contributor.departmentCHEMISTRY
dc.description.doi10.1002/marc.201000176
dc.description.sourcetitleMacromolecular Rapid Communications
dc.description.volume31
dc.description.issue17
dc.description.page1501-1508
dc.description.codenMRCOE
dc.identifier.isiut000282078800003
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