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Title: Decorating liquid crystal surfaces with proteins for real-time detection of specific protein-protein binding
Authors: Hartono, D. 
Xue, C.-Y.
Yang, K.-L. 
Yung, L.-Y.L. 
Issue Date: 23-Nov-2009
Citation: Hartono, 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.
Abstract: Here, 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.
Source Title: Advanced Functional Materials
ISSN: 1616301X
DOI: 10.1002/adfm.200901020
Appears in Collections:Staff Publications

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