dc.contributor.authorNallani, Madhavan
dc.contributor.authorDe Hoog, Hans-Peter M.
dc.contributor.authorCornelissen, Jeroen J. L. M.
dc.contributor.authorPalmans, Anja R. A.
dc.contributor.authorVan Hest, Jan C. M.
dc.contributor.authorNolte, Roeland J. M.
dc.date.accessioned2011-09-14T07:44:50Z
dc.date.available2011-09-14T07:44:50Z
dc.date.copyright2007en_US
dc.date.issued2007
dc.identifier.citationNallani, M., de Hoog, H. P. M., Cornelissen, J. J. L. M., Palmans, A. R. A., van Hest, J. C. M., & Nolte, R. J. M. (2007). Polymersome Nanoreactors for Enzymatic Ring-Opening Polymerization. Biomacromolecules, 8(12), 3723-3728.en_US
dc.identifier.issn1525-7797en_US
dc.identifier.urihttp://hdl.handle.net/10220/7050
dc.description.abstractPolystyrene-polyisocyanopeptide (PS-PIAT) polymersomes containing CALB in two different locations, one in the aqueous inner compartment and one in the bilayer, were investigated for enzymatic ring-opening polymerization of lactones in water. It is shown that the monomers 8-octanolactone and dodecalactone yield oligomers with this polymersome system. It is also observed that the polymerization activity is dependent on the position of the enzyme in the polymersome. SEM investigations show that the polymersome structures were destabilized during the polymerization. Further investigations show that the vesicular morphology of the polymersomes was destabilized only in the case of polymer product formation.en_US
dc.format.extent6 p.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesBiomacromoleculesen_US
dc.rights© 2007 American Chemical Societyen_US
dc.subjectDRNTU::Engineering::Materials::Biomaterials
dc.titlePolymersome nanoreactors for enzymatic ring-opening polymerizationen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Materials Science and Engineeringen_US
dc.identifier.doihttp://dx.doi.org/10.1021/bm7005938
dc.description.versionNone of the aboveen_US
dc.identifier.rims155290


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