Fluorinated glycosyl amino acids for mucin-like glycopeptide antigen analogues.
The aberrant glycosylation profiles of mucin glycoproteins on epithelial tumour cells represent attractive target structures for the development of immunotherapy against cancer. Mucin-type glycopeptides have been successfully investigated as molecularly defined vaccine prototypes for triggering humoral immunity but are susceptible to rapid in vivo degradation. As a potential means to enhance the bioavailabilities of the antigenic structures, hydrolysis-resistant carbohydrate analogues with fluorine substituents at positions C6, C2' and C6' were synthesised and incorporated into the tandem repeat sequence of the mucin MUC1. The resulting pseudo-glycopeptides can be used to elucidate the effects of chemically modified antibody determinants on metabolic and immunological properties.
Wagner
Sarah
S
Institut für Organische Chemie, Johannes Gutenberg-Universität Mainz, Duesbergweg 10-14, 55128 Mainz, Germany.
Mersch
Christian
C
Hoffmann-Röder
Anja
A
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry*; D015295:Antigens, Tumor-Associated, Carbohydrate / Q000737:chemistry* / Q000276:immunology*; D006020:Glycopeptides / Q000737:chemistry*; D006031:Glycosylation; D054879:Halogenation; D009682:Magnetic Resonance Spectroscopy; D018396:Mucin-1 / Q000737:chemistry* / Q000276:immunology; D009369:Neoplasms / Q000276:immunology; D013329:Structure-Activity Relationship
D000596:Amino Acids; D015295:Antigens, Tumor-Associated, Carbohydrate; D006020:Glycopeptides; D018396:Mucin-1