Premium
Towards Keratan Sulfate – Chemoenzymatic Cascade Synthesis of Sulfated N ‐Acetyllactosamine (LacNAc) Glycan Oligomers
Author(s) -
Lange Bastian,
Šimonová Anna,
Fischöder Thomas,
Pelantová Helena,
Křen Vladimír,
Elling Lothar
Publication year - 2016
Publication title -
advanced synthesis and catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.541
H-Index - 155
eISSN - 1615-4169
pISSN - 1615-4150
DOI - 10.1002/adsc.201500916
Subject(s) - sulfation , chemistry , glycan , keratan sulfate , oligomer , stereochemistry , glycosylation , linker , regioselectivity , biochemistry , carbohydrate conformation , glycoprotein , glycosaminoglycan , chondroitin sulfate , organic chemistry , nuclear magnetic resonance spectroscopy , catalysis , computer science , operating system
We report on a novel chemoenzymatic cascade for the synthesis of sulfated N ‐acetyllactosamine [(3Galβ1,4GlcNAcβ1,) n , LacNAc] oligomer structures. Starting from a linker modified GlcNAc substrate di‐ and trisaccharides were first synthesized by sequential use of human β4‐galactosyltransferase‐1 (β4GalT‐1) and β3‐ N ‐acetylglucosaminyltransferase from Helicobacter pylori (β3GlcNAcT). Subsequent regioselective chemical sulfation rendered the C‐6 mono‐, di‐, and tri‐ O ‐sulfated products in good yields. Further enzymatic elongation by β4GalT‐1 and β3GlcNAcT in a sequential mode yielded 6‐ O ‐sulfated LacNAc oligomers up to hexasaccharide length with variable degrees of sulfation. These carbohydrate structures mimic the sulfation pattern found in keratan sulfate and are potential ligands for different classes of glycan binding proteins.