Synthesis of tumor‐associated glycopeptide antigens for the development of tumor‐selective vaccines

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Abstract
In contrast to normal cells, the glycoprotein profile on epithelial tumor cells is distinctly altered. Due to an incomplete formation of the glycan side-chains resulting from a premature sialylation, additional peptide epitopes become accessible to the immune system in mucin-type glycoproteins on tumor cells. These tumor-associated structure alterations constitute the basis for a selective immunological attack on cancer cells. For the construction of immunostimulating antigens, glycopeptide partial structures from the mucins MUC1 and MUC4 carrying the tumor-associated sialyl-TN, α2,6-sialyl-T and α2,3-sialyl-T antigens have been synthesized. Employing different linkers such as the allylic HYCRON or the fluoride-sensitive PTMSEL anchor, the antigenic glycopeptide structures were constructed on the solid phase utilizing pre-assembled glycosyl amino acid building blocks prepared in solution by convergent chemical or chemoenzymatic strategies. The proliferation of cytotoxic T cells has been induced applying a construct composed of a sialyl-TN MUC1-glycopeptide conjugated with a tetanus toxin T cell peptide epitope. © 2004 The Japan Chemical Journal Forum and Wiley Periodicals, Inc. Chem Rec 3: 308–321, 2004: Published online in Wiley InterScience (www.interscience.wiley.com) DOI 10.1002/tcr10074

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