Use of Bacteriophage T7 Displayed Peptides for Determination of Monoclonal Antibody Specificity and Biosensor Analysis of the Binding Reaction

Direct kinetic assay of interactions between small peptides and immobilized antibodies using a surface plasmon resonance biosensor

“…1999 for interaction analysis has made it possible to obtain affinity and kinetic data for a large Ž number of antigen-antibody Brigham-Burke et al, 1992;VanCott et al, 1994;Oddie et al, 1997;. England et al, 1997;Houshmand et al, 1999, Ž . protein-protein Wu et al, 1995, protein-peptide Ž .…”

A Kinetic Study of Analyte–Receptor Binding and Dissociation, and Dissociation Alone, for Biosensor Applications: A Fractal Analysis

“…Houshmand et al (5) analyzed the binding and dissociation of 80 nM large T-antigen in solution to the monoclonal antibody, mAbLT1, immobilized on an SPR biosensor surface in the absence and in the presence of competitor peptide, NH 3 -CPNSLTPADPTMDY-COOH. After a time interval the injection of the protein ligand was interrupted, and the dissociation reaction was followed.…”

Applications of display technologies to proteomic analyses

“…Phage display technology was ®rst introduced in the middle of the 80s by Smith using Escherichia coli ®lamentous bacteriophage M13 [Smith, 1985]. Although several alternative phage display systems, such as l-phage, T4 and T7 phage [Santini et al, 1998;Ren and Black, 1998;Houshmand et al, 1999], have been developed for speci®c applications, M13 phage display is still the most robust method particularly applicable to small peptide and antibody engineering [Rader et al, 1998;Schmitz et al, 2000]. Applications of phage display technology in characterization of interactions between peptide ligands and ion-channel receptors have also been reported [Li, 1997].…”