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- Title
Enzymatic Synthesis of Spacer-Linked Divalent Glycosides Carrying N-Acetylglucosamine and N-Acetyllactosamine: Analysis of Cross-Linking Activities with WGA.
- Authors
Misawa, Yoshinori; Akimoto, Takashi; Amarume, Satoshi; Murata, Takeomi; Usui, Taichi
- Abstract
Divalent glycosides carrying N-acetyl-d-glucosamine (GlcNAc) and N-acetyllactosamine (LacNAc) were designed and prepared as glycomimetics. First, hexan-1,6-diyl bis-(2-acetamido-2-deoxy-β-d-glucopyranoside) (GlcNAc-Hx-GlcNAc) and 3,6-dioxaoct-1,8-diyl bis-(2-acetamido-2-deoxy-β-d-glucopyranoside) (GlcNAc-Doo-GlcNAc) were enzymatically synthesized by transglycosylation of an N,N′N″,N′″-tetraacetylchitotetraose [(GlcNAc)4] donor with a primary diol acceptor, utilizing a chitinolytic enzyme from Amycolatopsis orientalis. The resulting divalent glycosides were further converted to the respective hexan-1,6-diyl bis-[β-d-galactopyranosyl-(1→4)-2-acetamido-2-deoxy-β-d-glucopyranoside] (LacNAc-Hx-LacNAc) and 6-(2-acetamido-2-deoxy-β-d-glucopyranosyl)-hexyl β-d-galactopyranosyl-(1→4)-2-acetamido-2-deoxy-β-d-glucopyranoside (LacNAc-Hx-GlcNAc), and respective 3,6-dioxaoct-1,8-diyl bis-[β-d-galactopyranosyl-(1→4)-2-acetamido-2-deoxy-β-d-glucopyranoside] (LacNAc-Doo-LacNAc) and 8-(2-acetamido-2-deoxy-β-d-glucopyranosyl)-3,6-dioxaoctyl β-d-galactopyranosyl-(1→4)-2-acetamido-2-deoxy-β-d-glucopyranoside (LacNAc-Doo-GlcNAc) by galactosyltransferase. The interaction of wheat germ agglutinin (WGA) with a series of divalent glycosides and related compounds were studied using a biosensor based on surface plasmon resonance (SPR) and by precipitation analysis. Our results demonstrated that divalent glycosides carrying GlcNAc on both sides and GlcNAc and LacNAc on each side are capable of precipitating WGA as divalent ligands, but that the corresponding monovalent controls and divalent glycosides carrying LacNAc on both sides are unable to precipitate the lectin and bind as univalent ligands.
- Subjects
GLYCOSIDES; GLYCOASPARAGINASE; ENZYMES; DIOLEFINS; BIOCHEMISTRY
- Publication
Journal of Biochemistry, 2008, Vol 143, Issue 1, p21
- ISSN
0021-924X
- Publication type
Article
- DOI
10.1093/jb/mvm200