Abstract
Direct quantification of biomolecular interaction by single-molecule force spectroscopy has evolved into a powerful tool for materials and life sciences. We introduce an approach in which the unbinding forces required to break intermolecular bonds are measured in a differential format by comparison with a known reference bond (here, a short DNA duplex). In addition to a marked increase in sensitivity and force resolution, which enabled us to resolve single-base pair mismatches, this concept allows for highly specific parallel assays. This option was exploited to overcome cross-reactions of antibodies in a protein biochip application.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Antibodies
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Base Pair Mismatch*
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Biosensing Techniques*
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Carbocyanines
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Cross Reactions
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DNA* / chemistry
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DNA* / genetics
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DNA* / metabolism
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Dimethylpolysiloxanes
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Fluorescence
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Fluorescent Dyes
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Glass
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Humans
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Immunoassay
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Interleukin-5 / analysis
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Interleukin-5 / immunology
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Mice
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Microscopy, Atomic Force
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Nucleic Acid Conformation
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Nucleic Acid Hybridization
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Oligodeoxyribonucleotides / chemistry
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Oligodeoxyribonucleotides / metabolism
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Oligonucleotide Array Sequence Analysis*
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Protein Array Analysis*
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Protein Binding
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Silicones
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Temperature
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Thermodynamics
Substances
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Antibodies
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Carbocyanines
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Dimethylpolysiloxanes
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Fluorescent Dyes
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Interleukin-5
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Oligodeoxyribonucleotides
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Silicones
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cyanine dye 5
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baysilon
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DNA