6533b7d2fe1ef96bd125e2bb
RESEARCH PRODUCT
Effects of glycosylation on fragments of tumour associated human epithelial mucin MUC1.
Peter BraunPhilip M. WilliamsSaul J. B. TendlerHorst KunzG.mark DaviesMichael R. Pricesubject
Models MolecularGlycosylationGlycosylationMagnetic Resonance SpectroscopyStereochemistryProtein ConformationClinical BiochemistryMolecular Sequence DataPharmaceutical ScienceAlpha (ethology)Spectrometry Mass Fast Atom BombardmentBiochemistrychemistry.chemical_compoundProtein structureDrug DiscoveryHumansAmino Acid SequenceMolecular BiologyPeptide sequenceMUC1ChemistryOrganic ChemistryMucinMucin-1Nuclear magnetic resonance spectroscopyGlycopeptidePeptide Fragmentscarbohydrates (lipids)BiochemistryMolecular Medicinelipids (amino acids peptides and proteins)description
The glycodecapeptide AcPAPGS(alpha GalNAc)T(alpha GalNAc)APPA and the C-terminal glycohexapeptide AcS(alpha GalNAc)T(alpha GalNAc)APPA have been synthesized by applying the N-terminal Fmoc group in combination with the heptyl ester cleavable by lipase-catalyzed hydrolysis at pH 7. The solution conformation of these MUC1-related synthetic glycopeptides and the control, non-glycosylated decapeptide AcPAPGSTAPPA have been investigated using NMR spectroscopy. The structural studies indicate that the glycohexapeptide has a folded structure in solution. For this molecule, unrestrained molecular dynamics has been used to confirm the presence of the observed solution through-space connections. The results indicate that the non-globular nature of MUC1 is due to both protein core sequence and the effect of carbohydrate.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1998-11-05 | Bioorganicmedicinal chemistry |