{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,22]],"date-time":"2025-10-22T03:40:20Z","timestamp":1761104420527,"version":"build-2065373602"},"reference-count":19,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2006,2,3]],"date-time":"2006-02-03T00:00:00Z","timestamp":1138924800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["analyticalsciencejournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Proteomics"],"published-print":{"date-parts":[[2006,3]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Peptide microarrays displaying biologically active small synthetic peptides in a high\u2010density 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\u2010specific solution\u2010phase coupling of biotinylated synthetic peptides to NeutrAvidin (NA) and localized microdispensing of peptide\u2010NA\u2010complexes onto activated glass surfaces. Antibodies are captured in a sandwich manner between surface immobilized peptide probes and fluorescence\u2010labeled secondary antibodies. Our work includes a total of 54 peptides derived from immunodominant linear epitopes of the <jats:italic>T7 phage<\/jats:italic> capsid protein, <jats:italic>Herpes simplex virus<\/jats:italic> glycoprotein D, <jats:italic>c\u2010myc<\/jats:italic> protein, and three domains of the <jats:italic>Human coronavirus<\/jats:italic> polymerase polyprotein and their cognate mAbs. By using spacer molecules of different type and length for NA\u2010mediated 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\u2010picomolar concentrations of mAbs in buffered solutions and diluted human serum with high specificity.<\/jats:p>","DOI":"10.1002\/pmic.200500343","type":"journal-article","created":{"date-parts":[[2006,2,3]],"date-time":"2006-02-03T06:18:46Z","timestamp":1138947526000},"page":"1376-1384","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Functional peptide microarrays for specific and sensitive antibody diagnostics"],"prefix":"10.1002","volume":"6","author":[{"given":"Heiko","family":"Andresen","sequence":"first","affiliation":[]},{"given":"Carsten","family":"Gr\u00f6tzinger","sequence":"additional","affiliation":[]},{"given":"Kim","family":"Zarse","sequence":"additional","affiliation":[]},{"given":"Oliver J.","family":"Kreuzer","sequence":"additional","affiliation":[]},{"given":"Eva","family":"Ehrentreich\u2010F\u00f6rster","sequence":"additional","affiliation":[]},{"given":"Frank F.","family":"Bier","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2006,3,2]]},"reference":[{"doi-asserted-by":"publisher","key":"e_1_2_1_2_2","DOI":"10.1146\/annurev.biochem.72.121801.161511"},{"doi-asserted-by":"publisher","key":"e_1_2_1_3_2","DOI":"10.1126\/science.1062191"},{"key":"e_1_2_1_4_2","first-page":"864","volume-title":"Peptide Revolution: Genomics, Proteomics & Therapeutics","author":"Kreuzer O. 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