Please use this identifier to cite or link to this item: https://doi.org/10.1021/la2022215
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dc.titleLiquid crystal droplets as a hosting and sensing platform for developing immunoassays
dc.contributor.authorAliño, V.J.
dc.contributor.authorPang, J.
dc.contributor.authorYang, K.-L.
dc.date.accessioned2014-06-17T07:43:54Z
dc.date.available2014-06-17T07:43:54Z
dc.date.issued2011-10-04
dc.identifier.citationAliño, V.J., Pang, J., Yang, K.-L. (2011-10-04). Liquid crystal droplets as a hosting and sensing platform for developing immunoassays. Langmuir 27 (19) : 11784-11789. ScholarBank@NUS Repository. https://doi.org/10.1021/la2022215
dc.identifier.issn07437463
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/64156
dc.description.abstractIn this paper, we report an immunoassay in which probe proteins are immobilized on the surface of liquid crystal (LC) droplets rather than on solid surfaces. The advantage of this immunoassay is that the binding of antibodies to the probe proteins can be transduced by the LC droplets directly without the need for additional steps. For example, when we incubate the LC droplets decorated with immunoglobulin G (IgG) in a solution containing anti-IgG (AIgG), these droplets change their orientations from radial to bipolar configuration. In contrast, when we incubate the IgG-LC droplets in a solution containing anti-human serum albumin (AHSA), no changes are observed. The change of orientational configuration indicates the formation of the antigen-antibody immunocomplex on the surface of the LC droplets. Using LC droplet immunoassays, we successfully detect antibody concentrations as low as 0.01 μg/mL for AIgG and 0.02 μg/mL for AHSA. Because the immunoassay using LC droplets is label-free and gives a unique optical response, it has the potential to be further developed as a portable and low-cost immunoassay. © 2011 American Chemical Society.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1021/la2022215
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentCHEMICAL & BIOMOLECULAR ENGINEERING
dc.description.doi10.1021/la2022215
dc.description.sourcetitleLangmuir
dc.description.volume27
dc.description.issue19
dc.description.page11784-11789
dc.description.codenLANGD
dc.identifier.isiut000295187300010
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