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Design and application of a microarray for fluorescence and and Surface Plasmon Resonance imaging analysis of peptide-antibody interactions.

Abstract : In the past few years, protein and peptide microarrays have shown a great potential in fundamental research, medical diagnostics and drug discovery. We have developed a new method based on covalent immobilization of peptides on a microarray gold surface for detecting antibodies by either fluorescence or surface plasmon resonance imaging (SPRi). The fluorescence-based revelation approach allows for an indirect analysis of protein-antibody binding via labeled molecules, whereas the SPRi-based assay is a real-time and label-free detection system suitable for the direct analysis of biological interactions. We illustrate our peptide chip's efficiency in specifically binding serum antibodies and compare the fluorescence and SPRi approaches to detect peptide-antibody interactions. Moreover, we used a monoclonal antibody against the hepatitis C virus nucleocapsid protein to provide evidence that our system is a powerful tool to identify which epitope is recognized by a given antibody. This novel technology therefore provides a promising tool for both antibody screening and epitope mapping.
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https://www.hal.inserm.fr/inserm-00267060
Contributor : Marie-Bernadette Villiers <>
Submitted on : Wednesday, March 26, 2008 - 12:42:33 PM
Last modification on : Friday, November 6, 2020 - 4:04:57 AM

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Boutheina Cherif, Christian Villiers, Glaucia Paranhos-Baccalà, Roberto Calemczuk, Patrice Marche, et al.. Design and application of a microarray for fluorescence and and Surface Plasmon Resonance imaging analysis of peptide-antibody interactions.. Journal of Biomedical Nanotechnology, American Scientific Publishers, 2006, 2 (1), pp.29-35. ⟨10.1166/jbn.2006.005⟩. ⟨inserm-00267060⟩

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