Please use this identifier to cite or link to this item: https://doi.org/10.1002/adfm.200901020
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
Source: 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

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

54
checked on Feb 22, 2018

WEB OF SCIENCETM
Citations

52
checked on Jan 22, 2018

Page view(s)

30
checked on Feb 19, 2018

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.