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Clinically Related Protein–Peptide Interactions Monitored in Real Time on Novel Peptide Chips by Surface Plasmon Resonance Imaging

¹ Laboratoire d’Immunochimie, Commissariat à L’Energie Atomique (CEA)-Grenoble/Départment Réponse et Dynamique Cellulaire (DRDC), Institut National de la Santé et de la Recherche Médicale (INSERM) U548, Université J. Fourier (UJF), Grenoble, France.
² Chimie de la Reconnaissance et Etude des Assemblages Biologiques (CEA, Centre National de la Recherche Scientifique, UJF), CEA-Grenoble/Départment de Recherche Fondamentale sur la Matiére Condenseé, Unité Mixte de Recherche 5819, Grenoble, France.
³ Département d’Hépato-Gastroentérologie, CHU de Grenoble, Grenoble, France.

^aAddress correspondence to this author at: INSERM U548, DRDC/ICH, CEA-Grenoble, 17 Rue des Martyrs, F-38054 Grenoble, France. Fax 33-4-38-78-98-03; e-mail immuno{at}dsvgre.cea.fr.

Background: Developing rapid, high-throughput assays for detecting and characterizing protein–protein interactions is a great challenge in the postgenomic era. We have developed a new method that allows parallel analysis of multiple analytes in biological fluids and is suitable for biological and medical studies.

Methods: This technology for studying peptide–antibody interactions is based on polypyrrole-peptide chips and surface plasmon resonance imaging (SPRi). We generated a chip bearing a large panel of peptide probes by successive electro-directed copolymerizations of pyrrole–peptide conjugates on a gold surface.

Results: We provide evidence that (a) the signal produced by antibody binding is highly specific; (b) the detected signal specifically reflects the antibody concentration of the tested solution in a dose-dependent manner; (c) this technique is appropriate for analyzing complex media such as undiluted sera, a novelty with respect to previous techniques; and (d) correlation between classic ELISA results and the SPRi signal is good (P = 0.008). We also validated this system in a medical model by detecting anti-hepatitis C antibodies in patient-derived sera.

Conclusion: Because of its characteristics (easy preparation of the peptide chip; high-throughput, label-free, real-time detection; high specificity; and low background), this technology is suitable for screening biological samples and for large-scale studies.

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				D. Tang, R. Yuan, and Y. Chai Magnetic Control of an Electrochemical Microfluidic Device with an Arrayed Immunosensor for Simultaneous Multiple Immunoassays Clin. Chem., July 1, 2007; 53(7): 1323 - 1329. [Abstract] [Full Text] [PDF]