Journal
ADVANCED FUNCTIONAL MATERIALS
Volume 19, Issue 22, Pages 3574-3579Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/adfm.200901020
Keywords
-
Categories
Funding
- National University of Singapore (NUS) [R-279-000-205-112, R279-000-282112]
- AUN/SEED-Net JICA
Ask authors/readers for more resources
Here, a novel method of immobilizing proteins with well-define orientation directly on liquid crystal surfaces that allow subsequent real-time imaging of specific protein-protein binding events on these surfaces is reported. Self- assembly of nitrilotriacetic acid terminated amphiphiles loaded with Ni2+ ions at aqueous-liquid crystal interface creates a surface capable of immobilizing histidine-tagged ubiquitin through complex formation between Ni2+ and histidine. When these surfaces containing immobilized histidine- tagged 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available