Identification of peptide sequences that bind the Thomsen-Friedenreich cancer-associated glycoantigen from bacteriophage peptide display libraries |
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Authors: | Elena N Peletskaya Gennadi Glinsky Susan L Deutscher Thomas P Quinn |
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Institution: | (1) Department of Biochemistry, University of Missouri, 65211 Columbia, MO, USA;(2) Cancer Research Center, 350 Berrywood Drive, 65201 Columbia, MO, USA |
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Abstract: | Summary The goal of this study was to determine if polypeptides that bind specifically to the carcinoma-associated Thomsen-Friedenreich (T) antigen could be isolated from a random peptide bacteriophage display library. T antigen is a carbohydrate antigen that is exposed and immunoreactive on the surfaces of most primary carcinomas and their metastases, while it is masked on normal cells. Tumor-specific surface carbohydrates are often used as markers of cell differentiation and play a role in cell aggregation, which is an important step in the metastatic process. Therefore, peptides that bind and mask T antigen may yield useful carbohydrate-specific probes and provide insight into carbohydrate-mediated tumor-cell aggregation. A 15-amino acid random peptide bacteriophage display library was screened for polypeptides that exhibited high specificity to two glycoproteins which display T antigen on their surfaces. The results suggest that synthetic peptides identified from the bacteriophage display library have high affinities (Kd 1 M) and specificities for proteins and human tumor cells which present T antigen. Thus, random bacteriophage peptide display libraries may be a rich source of sequences that bind to carbohydrate antigen structures. |
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Keywords: | Cancer-associated glycoantigen Thomsen-Friedenreich antigen Random peptide libraries Bacteriophage display Peptide-carbohydrate interactions |
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