Solid-phase synthesis and conformational studies of glycosylated derivatives of helper-T-cell immunogenic peptides from hen-egg lysozyme.
3-Mercaptopropionic acid and N alpha-Fmoc serine, both with unprotected carboxyl groups, were stereospecifically glycosylated in 62-82% yields, using saccharide 1,2-trans peracetates and Lewis acid catalysis. The resulting glycosylated building blocks were used in the synthesis of derivatives of helper-T-cell stimulating peptides, with the carbohydrate moiety located at the amino terminus, or internally in the peptide chain. 1H NMR spectroscopy in Me2SO-d6 showed that the glycopeptides assumed random conformations, which were not influenced by the glycosylation or by single substitutions of amino acids in the peptide moiety.
Elofsson
M
M
Lund Institute of Technology, Sweden.
Roy
S
S
Walse
B
B
Kihlberg
J
J
D000595:Amino Acid Sequence; D000818:Animals; D000941:Antigens / Q000737:chemistry*; D002240:Carbohydrate Sequence; D002645:Chickens; D006020:Glycopeptides / Q000138:chemical synthesis*; D006031:Glycosylation; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry*; D010063:Ovum / Q000201:enzymology; D010446:Peptide Fragments / Q000737:chemistry*; D006377:T-Lymphocytes, Helper-Inducer / Q000276:immunology
D000941:Antigens; D006020:Glycopeptides; D010446:Peptide Fragments; D009113:Muramidase