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|Title:||Decorating liquid crystal surfaces with proteins for real-time detection of specific protein-protein binding||Authors:||Hartono, D.
|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. https://doi.org/10.1002/adfm.200901020||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||URI:||http://scholarbank.nus.edu.sg/handle/10635/88732||ISSN:||1616301X||DOI:||10.1002/adfm.200901020|
|Appears in Collections:||Staff Publications|
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