Chemoenzymatic synthesis of neoglycopeptides: application to an alpha-Gal-terminated neoglycopeptide.
A novel methodology for the enzymatic preparation from suitably derivatized oligosaccharides of N-linked neoglycopeptides using the microbial glutaminyl-peptide gamma-glutamyl transferase, transglutaminase (TGase), is described. N-Allyl glycosides of various oligosaccharides were photochemically coupled with cysteamine to yield amino-terminated thioether spacers, which were accepted by transglutaminase to transamidate the side-chain gamma-carboxamide group in the dipeptide Z-Gln-Gly.
Ramos
D
D
Unilever Research Laboratory Vlaardingen, Olivier van Noortlaan 120, NL-3313AT Vlaardingen, The Netherlands.
Rollin
P
P
Klaffke
W
W
D000215:Acylation; D000641:Ammonia / Q000737:chemistry; D002241:Carbohydrates / Q000737:chemistry; D002855:Chromatography, Thin Layer; D003543:Cysteamine / Q000737:chemistry; D005973:Glutamine / Q000737:chemistry; D006020:Glycopeptides / Q000138:chemical synthesis*; D007202:Indicators and Reagents; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D017510:Protein Folding; D013056:Spectrophotometry, Ultraviolet
D002241:Carbohydrates; D006020:Glycopeptides; D007202:Indicators and Reagents; D005973:Glutamine; D003543:Cysteamine; D000641:Ammonia