title: Effects of glycosylation on fragments of tumour associated human epithelial mucin MUC1.
abstract: 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.
authors.affiliation: Institut für Organische Chemie, Universität Mainz, Germany.
authors.forename: P
authors.initials: P
authors.lastname: Braun
authors.forename: G M
authors.initials: GM
authors.lastname: Davies
authors.forename: M R
authors.initials: MR
authors.lastname: Price
authors.forename: P M
authors.initials: PM
authors.lastname: Williams
authors.forename: S J
authors.initials: SJ
authors.lastname: Tendler
authors.forename: H
authors.initials: H
authors.lastname: Kunz
mesh_terms: D000595:Amino Acid Sequence; D006031:Glycosylation; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D018396:Mucin-1 / Q000737:chemistry / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism*; D011487:Protein Conformation; D016339:Spectrometry, Mass, Fast Atom Bombardment
chemical_list: D018396:Mucin-1; D010446:Peptide Fragments