Journal of Protein Chemistry

, Volume 21, Issue 4, pp 287-296

First online:

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

  • Natalia G. KarassevaAffiliated withDepartment of Biochemistry, University of Missouri
  • , Vladislav V. GlinskyAffiliated withDepartment of Biochemistry, University of Missouri
  • , Ning X. ChenAffiliated withDepartment of Biochemistry, University of Missouri
  • , Ravichandra KomatireddyAffiliated withDepartment of Biochemistry, University of Missouri
  • , Thomas P. QuinnAffiliated withDepartment of Biochemistry, University of Missouri Email author 

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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.

Bacteriophage display synthetic peptides ErbB-2 human carcinomas