Normal mucin is a class of large heavily glycosylated protein that is expressed on apical epithelial cell surfaces. Tumor mucin contains reduced carbohydrate chains that induces an immunologic response. This study may have implications in the area of peptide epitope-protein carrier complex for invoking the immune system.  In this study we investigated to see whether or not a shortened mucin peptide epitope and substituted mucin peptides will still be recognized by specific antibody.  Results showed that mucin specific monoclonal antibody has some affinity to GVTSAFD but none to GVTSALD and GVTSADD.  The data showed that the shortened version of mucin peptide epitope (GVTSAPD) still is recognized by Muc-1 specific monoclonal antibody.  The epitope interactions observed by STD-NMR occurred at the methyl groups of V2, T3 and A5, and the Ha and H? of P6.  The saturation transfer of other Ha's is much weaker compared to the Ha of Pro.

Antibody binding study of mucin peptide epitopes

243rd National Meeting (2012)

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