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Immunoassay, DNA Analysis, and Other Ligand Binding Assay Techniques: From Electropherograms to Multiplexed, Ultrasensitive Microarrays on a Chip
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Abstract
"Ligand" or "binding" assays have made a major impact on biomedical research and clinical diagnosis since their development in the late 1950s. Immunoassay techniques (relying on specific antibodies to bind the target analyte) represent the best-known example, but analogous DNA and RNA analysis methods (using oligonucleotides to recognize defined polynucleotide sequences) are rapidly gaining in importance and are likely to exert profound effects on human society.
The evolution of these methods may be divided into three phases: (i) the initial development and widespread use of sensitive "competitive" assays relying on radioisotopically labeled analyte to monitor the binding reaction; (ii) the introduction in the 1980s of "ultrasensitive", "noncompetitive", labeled antibody methods relying on high-specific-activity nonisotopic labels, leading to the emergence of the automatic analyzers that now dominate the field, and (iii) the present development of "microarray"methods based on antibody or oligonucleotide microspots (each recognizing an individual analyte) arrayed on a solid support and relying on observation (typically by confocal microscopy) of fluorescent signals emitted from each spot.
Miniaturized microarray methods permitting ultrasensitive measurement of hundreds of different analytes in a minute sample are likely to revolutionize medicine and related fields within the next decade.
Keywords (Audience):
Second-Year UndergraduateKeywords (Domain):
Analytical ChemistryKeywords (Subject):
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This article has been cited by 4 ACS Journal articles (4 most recent appear below).
Significance of Antibody Orientation Unraveled: Well-Oriented Antibodies Recorded High Binding Affinity
Nobuyuki Tajima, Madoka Takai, and Kazuhiko IshiharaAnalytical Chemistry2011 83 (6), 1969-1976Significance of Antibody Orientation Unraveled: Well-Oriented Antibodies Recorded High Binding Affinity
Nobuyuki Tajima, Madoka Takai, and Kazuhiko IshiharaAnalytical Chemistry2011 83 (6), 1969-1976To investigate the effect of antibody orientation on its immunological activities, we developed a novel and versatile platform consisting of a well-defined phospholipid polymer surface on which staphylococcal protein A (SpA) was site-selectively ...
Complementary Spectroscopic Assays for Investigating Protein−Ligand Binding Activity: A Project for the Advanced Chemistry Laboratory
David P. Mascotti and Mark J. WanerJournal of Chemical Education2010 87 (7), 735-738Complementary Spectroscopic Assays for Investigating Protein−Ligand Binding Activity: A Project for the Advanced Chemistry Laboratory
David P. Mascotti and Mark J. WanerJournal of Chemical Education2010 87 (7), 735-738A protein−ligand binding, guided-inquiry laboratory project with potential application across the advanced undergraduate curriculum is described. At the heart of the project are fluorescence and spectrophotometric assays utilizing biotin-4-fluorescein and ...
Utilization of Kinetically Enhanced Monovalent Binding Affinity by Immunoassays Based on Multivalent Nanoparticle-Antibody Bioconjugates
Tero Soukka, Harri Härmä, Janika Paukkunen, and Timo LövgrenAnalytical Chemistry2001 73 (10), 2254-2260Utilization of Kinetically Enhanced Monovalent Binding Affinity by Immunoassays Based on Multivalent Nanoparticle-Antibody Bioconjugates
Tero Soukka, Harri Härmä, Janika Paukkunen, and Timo LövgrenAnalytical Chemistry2001 73 (10), 2254-2260The monovalent binding affinity of high binding site density nanoparticle−antibody bioconjugates is shown to exceed the intrinsic affinity of the original, monoclonal antibody. The nanoparticle−antibody bioconjugates were prepared by covalent coupling of ...
Noncompetitive Immunoassay of Small Analytes at the Femtomolar Level by Affinity Probe Capillary Electrophoresis: Direct Analysis of Digoxin Using a Uniform-Labeled scFv Immunoreagent
Frank T. Hafner, Roger A. Kautz, Brent L. Iverson, Roger C. Tim, and Barry L. KargerAnalytical Chemistry2000 72 (23), 5779-5786Noncompetitive Immunoassay of Small Analytes at the Femtomolar Level by Affinity Probe Capillary Electrophoresis: Direct Analysis of Digoxin Using a Uniform-Labeled scFv Immunoreagent
Frank T. Hafner, Roger A. Kautz, Brent L. Iverson, Roger C. Tim, and Barry L. KargerAnalytical Chemistry2000 72 (23), 5779-5786A general method for noncompetitive immunoassay of small analytes using affinity probe capillary electrophoresis (APCE) is demonstrated using digoxin as a model analyte. A uniform immunoreagent was prepared from a single-chain antibody (scFv) gene ...
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- Received: August 03, 2009
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