Publication Date:
1998-04-16
Description:
Liquid crystals (LCs) were used to amplify and transduce receptor-mediated binding of proteins at surfaces into optical outputs. Spontaneously organized surfaces were designed so that protein molecules, upon binding to ligands hosted on these surfaces, triggered changes in the orientations of 1- to 20-micrometer-thick films of supported LCs, thus corresponding to a reorientation of approximately 10(5) to 10(6) mesogens per protein. Binding-induced changes in the intensity of light transmitted through the LC were easily seen with the naked eye and could be further amplified by using surfaces designed so that protein-ligand recognition causes twisted nematic LCs to untwist. This approach to the detection of ligand-receptor binding does not require labeling of the analyte, does not require the use of electroanalytical apparatus, provides a spatial resolution of micrometers, and is sufficiently simple that it may find use in biochemical assays and imaging of spatially resolved chemical libraries.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gupta, V K -- Skaife, J J -- Dubrovsky, T B -- Abbott, N L -- New York, N.Y. -- Science. 1998 Mar 27;279(5359):2077-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Engineering and Materials Science, University of California, Davis, CA 95616, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9516101" target="_blank"〉PubMed〈/a〉
Keywords:
Anisotropy
;
Antigen-Antibody Reactions
;
Avidin/*metabolism
;
Biotin/immunology/*metabolism
;
Biotinylation
;
Crystallization
;
Gold
;
Immunoglobulin G/*metabolism
;
Ligands
;
*Optics and Photonics
;
*Protein Binding
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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