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dc.contributor.authorSutisna, Burhannudin
dc.contributor.authorPolymeropoulos, Georgios
dc.contributor.authorMygiakis, E.
dc.contributor.authorMusteata, Valentina-Elena
dc.contributor.authorPeinemann, Klaus-Viktor
dc.contributor.authorSmilgies, D. M.
dc.contributor.authorHadjichristidis, Nikos
dc.contributor.authorNunes, Suzana Pereira
dc.date.accessioned2016-12-13T06:46:50Z
dc.date.available2016-12-13T06:46:50Z
dc.date.issued2016
dc.identifier.citationSutisna B, Polymeropoulos G, Mygiakis E, Musteata V, Peinemann K-V, et al. (2016) Artificial membranes with selective nanochannels for protein transport. Polym Chem 7: 6189–6201. Available: http://dx.doi.org/10.1039/c6py01401a.
dc.identifier.issn1759-9954
dc.identifier.issn1759-9962
dc.identifier.doi10.1039/c6py01401a
dc.identifier.urihttp://hdl.handle.net/10754/622006
dc.description.abstractA poly(styrene-b-tert-butoxystyrene-b-styrene) copolymer was synthesized by anionic polymerization and hydrolyzed to poly(styrene-b-4-hydroxystyrene-b-styrene). Lamellar morphology was confirmed in the bulk after annealing. Membranes were fabricated by self-assembly of the hydrolyzed copolymer in solution, followed by water induced phase separation. A high density of pores of 4 to 5 nm diameter led to a water permeance of 40 L m−2 h−1 bar−1 and molecular weight cut-off around 8 kg mol−1. The morphology was controlled by tuning the polymer concentration, evaporation time, and the addition of imidazole and pyridine to stabilize the terpolymer micelles in the casting solution via hydrogen bond complexes. Transmission electron microscopy of the membrane cross-sections confirmed the formation of channels with hydroxyl groups beneficial for hydrogen-bond forming sites. The morphology evolution was investigated by time-resolved grazing incidence small angle X-ray scattering experiments. The membrane channels reject polyethylene glycol with a molecular size of 10 kg mol−1, but are permeable to proteins, such as lysozyme (14.3 kg mol−1) and cytochrome c (12.4 kg mol−1), due to the right balance of hydrogen bond interactions along the channels, electrostatic attraction, as well as the right pore sizes. Our results demonstrate that artificial channels can be designed for protein transport via block copolymer self-assembly using classical methods of membrane preparation.
dc.description.sponsorshipThis work was funded by the King Abdullah University of Science and Technology (KAUST) Grant 1671 – CRG2. The authors thank Dr Yihui Xie and Dr Stefan Chisca for the discussion on polymer modification and NMR analysis, as well as CHESS at Cornell, USA and LNLS in Brazil for access to the GISAXS and SAXS synchrotron facilities. The Cornell High Energy Synchrotron Source (CHESS) is supported by the National Science Foundation and the National Institutes of Health/National Institute of General Medical Sciences under NSF award DMR-1332208.
dc.publisherRoyal Society of Chemistry (RSC)
dc.relation.urlhttp://pubs.rsc.org/en/Content/ArticleLanding/2016/PY/C6PY01401A
dc.rightsArchived thanks to the Royal Society of Chemistry
dc.titleArtificial membranes with selective nanochannels for protein transport
dc.typeArticle
dc.contributor.departmentAdvanced Membranes and Porous Materials Research Center
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentChemical Engineering Program
dc.contributor.departmentChemical Science Program
dc.contributor.departmentEnvironmental Science and Engineering Program
dc.contributor.departmentKAUST Catalysis Center (KCC)
dc.contributor.departmentNanostructured Polymeric Membrane Lab
dc.contributor.departmentPhysical Science and Engineering (PSE) Division
dc.contributor.departmentPolymer Synthesis Laboratory
dc.contributor.departmentWater Desalination and Reuse Research Center (WDRC)
dc.identifier.journalPolym. Chem.
dc.eprint.versionPost-print
dc.contributor.institutionCornell High Energy Synchrotron Source, Wilson Laboratory, Cornell University, Ithaca, New York 14853, USA
kaust.personSutisna, Burhannudin
kaust.personPolymeropoulos, Georgios
kaust.personMygiakis, E.
kaust.personMusteata, Valentina-Elena
kaust.personPeinemann, Klaus-Viktor
kaust.personHadjichristidis, Nikos
kaust.personNunes, Suzana Pereira
kaust.grant.number1671 – CRG2
refterms.dateFOA2017-09-04T00:00:00Z


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