Functional peptide microarrays for specific and sensitive antibody diagnostics
Identifieur interne : 002E32 ( Main/Exploration ); précédent : 002E31; suivant : 002E33Functional peptide microarrays for specific and sensitive antibody diagnostics
Auteurs : Heiko Andresen [Allemagne] ; Carsten Grötzinger [Allemagne] ; Kim Zarse [Allemagne] ; Oliver J. Kreuzer [Allemagne] ; Eva Ehrentreich-Förster [Allemagne] ; Frank F. Bier [Allemagne]Source :
- PROTEOMICS [ 1615-9853 ] ; 2006-03.
English descriptors
- Teeft :
- Amino, Amino acids, Antibody, Antibody affinity, Antibody binding, Antibody detection, Antibody incubations, Assay, Binding sites, Biological function, Biomedical engineering, Biotinylated peptides, Blood samples, Carrier protein, Cognate mabs, Contrast values, Data evaluation, Detection limit, Diagnostic assay, Different type, Epitope, Epitope mapping approach, Fluorescence imaging, Fluorescence intensities, Fluorescence signals, Fraunhofer institute, Free peptide ligand, Glass slides, Glass surfaces, Gmbh, Herpes simplex virus glycoprotein, Higher sbrs, Human serum, Hydrogen phosphate, Immobilization, Immobilization direction, Incubation control, Kgaa, Ligand, Limited sensitivity, Liquid samples, Localized microdispensing, Mabs, Merck biosciences, Microarray, Microarrays, Minimum spacer length, Moist chambers, Molecular bioanalytics bioelectronics, Monoclonal mouse antibody, Other mabs, Peptide, Peptide antigens, Peptide array, Peptide arrays, Peptide immobilization direction, Peptide ligands, Peptide microarray, Peptide microarrays, Peptide probe, Peptide probes, Phage capsid protein, Physicochemical properties, Pnac spots, Pnacs, Point temperature, Potassium chloride, Potassium phosphate, Primary antibodies, Probe, Protein microarrays, Proteomics, Reference spots, Relative fluorescence units, Room temperature, Sbrs, Sciflex arrayer, Secondary antibody, Secondary importance, Serial dilutions, Sodium chloride, Spacer, Spacer incorporation, Spacer moiety, Spacer molecule, Spacer molecules, Spacer type, Synthetic peptides, Target molecules, Technology proteomics, Unbound peptides, Verlag, Verlag gmbh, Weinheim.
Abstract
Peptide microarrays displaying biologically active small synthetic peptides in a high‐density format provide an attractive technology to probe complex samples for the presence and/or function of protein analytes. We present a new approach for manufacturing functional peptide microarrays for molecular immune diagnostics. Our method relies on the efficiency of site‐specific solution‐phase coupling of biotinylated synthetic peptides to NeutrAvidin (NA) and localized microdispensing of peptide‐NA‐complexes onto activated glass surfaces. Antibodies are captured in a sandwich manner between surface immobilized peptide probes and fluorescence‐labeled secondary antibodies. Our work includes a total of 54 peptides derived from immunodominant linear epitopes of the T7 phage capsid protein, Herpes simplex virus glycoprotein D, c‐myc protein, and three domains of the Human coronavirus polymerase polyprotein and their cognate mAbs. By using spacer molecules of different type and length for NA‐mediated peptide presentation, we show that the incorporation of a minimum spacer length is imperative for antibody binding, whereas the peptide immobilization direction has only secondary importance for antibody affinity and binding. We further demonstrate that the peptide array is capable of detecting low‐picomolar concentrations of mAbs in buffered solutions and diluted human serum with high specificity.
Url:
DOI: 10.1002/pmic.200500343
Affiliations:
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We present a new approach for manufacturing functional peptide microarrays for molecular immune diagnostics. Our method relies on the efficiency of site‐specific solution‐phase coupling of biotinylated synthetic peptides to NeutrAvidin (NA) and localized microdispensing of peptide‐NA‐complexes onto activated glass surfaces. Antibodies are captured in a sandwich manner between surface immobilized peptide probes and fluorescence‐labeled secondary antibodies. Our work includes a total of 54 peptides derived from immunodominant linear epitopes of the T7 phage capsid protein, Herpes simplex virus glycoprotein D, c‐myc protein, and three domains of the Human coronavirus polymerase polyprotein and their cognate mAbs. By using spacer molecules of different type and length for NA‐mediated peptide presentation, we show that the incorporation of a minimum spacer length is imperative for antibody binding, whereas the peptide immobilization direction has only secondary importance for antibody affinity and binding. We further demonstrate that the peptide array is capable of detecting low‐picomolar concentrations of mAbs in buffered solutions and diluted human serum with high specificity.</div></front></TEI><affiliations><list><country><li>Allemagne</li></country><region><li>Berlin</li><li>Brandebourg</li></region><settlement><li>Berlin</li><li>Potsdam</li></settlement><orgName><li>Université de Potsdam</li></orgName></list><tree><country name="Allemagne"><noRegion><name sortKey="Andresen, Heiko" sort="Andresen, Heiko" uniqKey="Andresen H" first="Heiko" last="Andresen">Heiko Andresen</name></noRegion><name sortKey="Andresen, Heiko" sort="Andresen, Heiko" uniqKey="Andresen H" first="Heiko" last="Andresen">Heiko Andresen</name><name sortKey="Bier, Frank F" sort="Bier, Frank F" uniqKey="Bier F" first="Frank F." last="Bier">Frank F. Bier</name><name sortKey="Bier, Frank F" sort="Bier, Frank F" uniqKey="Bier F" first="Frank F." last="Bier">Frank F. Bier</name><name sortKey="Ehrentreich Rster, Eva" sort="Ehrentreich Rster, Eva" uniqKey="Ehrentreich Rster E" first="Eva" last="Ehrentreich-Förster">Eva Ehrentreich-Förster</name><name sortKey="Grotzinger, Carsten" sort="Grotzinger, Carsten" uniqKey="Grotzinger C" first="Carsten" last="Grötzinger">Carsten Grötzinger</name><name sortKey="Grotzinger, Carsten" sort="Grotzinger, Carsten" uniqKey="Grotzinger C" first="Carsten" last="Grötzinger">Carsten Grötzinger</name><name sortKey="Kreuzer, Oliver J" sort="Kreuzer, Oliver J" uniqKey="Kreuzer O" first="Oliver J." last="Kreuzer">Oliver J. Kreuzer</name><name sortKey="Zarse, Kim" sort="Zarse, Kim" uniqKey="Zarse K" first="Kim" last="Zarse">Kim Zarse</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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