Please use this identifier to cite or link to this item: https://doi.org/10.1002/adfm.200901020
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dc.titleDecorating liquid crystal surfaces with proteins for real-time detection of specific protein-protein binding
dc.contributor.authorHartono, D.
dc.contributor.authorXue, C.-Y.
dc.contributor.authorYang, K.-L.
dc.contributor.authorYung, L.-Y.L.
dc.date.accessioned2014-10-09T06:45:41Z
dc.date.available2014-10-09T06:45:41Z
dc.date.issued2009-11-23
dc.identifier.citationHartono, D., Xue, C.-Y., Yang, K.-L., Yung, L.-Y.L. (2009-11-23). Decorating liquid crystal surfaces with proteins for real-time detection of specific protein-protein binding. Advanced Functional Materials 19 (22) : 3574-3579. ScholarBank@NUS Repository. https://doi.org/10.1002/adfm.200901020
dc.identifier.issn1616301X
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/88732
dc.description.abstractHere, a novel method of immobilizing proteins with well-defined orientation directly on liquid crystal surfaces that allow subsequent real-time imaging of specific protein-protein binding events on these surfaces is reported. Selfassembly of nitrilotriacetic acid terminated amphiphiles loaded with Ni 2+ ons at aqueous-liquid crystal interface creates a surface capable of immobilizing histidine-tagged ubiquittn through complex formation between Ni2+ and histidine. When these surfaces containing immobilized histidinetagged ubiquitin are exposed to anti-ubiquitin antibody, the spatial and temporal of specific protein-protein binding events trigger orientational transitions of liquid crystals. As a result, sharp liquid crystal optical switching from dark to bright can readily be observed under polarized lighting. The protein-protein binding can be observed within seconds and only requires nanogram quantities of proteins. This work demonstrates a simple strategy to immobilize proteins with well-defined orientation on liquid crystal surfaces for real-time and label-free detection of specific protein-protein binding events, which may find use in biomedical diagnostics © 2009 WILEY-VCH Verlag GmbH & Co. KGaA.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1002/adfm.200901020
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentCHEMICAL & BIOMOLECULAR ENGINEERING
dc.description.doi10.1002/adfm.200901020
dc.description.sourcetitleAdvanced Functional Materials
dc.description.volume19
dc.description.issue22
dc.description.page3574-3579
dc.description.codenAFMDC
dc.identifier.isiut000272503500007
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