6533b82ffe1ef96bd12951ed
RESEARCH PRODUCT
Fluorinated glycosyl amino acids for mucin-like glycopeptide antigen analogues.
Sarah WagnerAnja Hoffmann-röderChristian Merschsubject
GlycosylationMagnetic Resonance SpectroscopyHalogenationCatalysischemistry.chemical_compoundStructure-Activity RelationshipAntigenNeoplasmsGlycosylAntigens Tumor-Associated CarbohydrateAmino Acid SequenceAmino AcidsMUC1chemistry.chemical_classificationbiologyOrganic ChemistryMucinMucin-1GlycopeptidesGeneral ChemistryGlycopeptideAmino acidchemistryBiochemistrybiology.proteinAntibodyGlycoproteindescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2010-05-12 | Chemistry (Weinheim an der Bergstrasse, Germany) |