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Identification and Characterization of Peptides That Bind Human ErbB-2 Selected from a Bacteriophage Display Library

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Abstract

The ErbB-2 receptor, a member of the tyrosine kinase type 1 family of receptors, has been implicated in many human malignancies. The overexpression of ErbB-2 in cancer cells as well as its extracellular accessibility makes it an attractive target for the development of tumor-specific agents. In this study, random peptide bacteriophage display technology was employed to identify peptides that bound the extracellular domain of human ErbB-2. The peptide KCCYSL, most frequently occurring in the affinity-selected phage population, was chemically synthesized and characterized for its binding activities to ErbB-2. The synthetic peptide exhibited high specificity for ErbB-2 and an equilibrium dissociation constant of 30 μM. Peptide binding to ErbB-2 positive human breast and prostate carcinoma cells was visualized in direct cell binding assays. In conclusion, the peptide KCCYSL has the potential to be developed into a cancer imaging or therapeutic agent targeting malignant cells overexpressing the ErbB-2 receptor.

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Correspondence to Thomas P. Quinn.

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Karasseva, N.G., Glinsky, V.V., Chen, N.X. et al. Identification and Characterization of Peptides That Bind Human ErbB-2 Selected from a Bacteriophage Display Library. J Protein Chem 21, 287–296 (2002). https://doi.org/10.1023/A:1019749504418

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  • DOI: https://doi.org/10.1023/A:1019749504418

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