1314746-09-2

Upstream product

• 923952-61-8 2-azido-2-deoxy-4,6-O-(2-naphthylmethylidene)-β-D-glucopyranosyl benzoate 
• 589-15-1 1-bromomethyl-4-bromobenzene 
• 1374562-18-1 C₄₇H₄₆BrN₃O₆Si 
• 1374562-16-9 C₃₁H₂₆BrN₃O₆ 
• 1374562-19-2 2-azido-3-O-(4-bromobenzyl)-6-O-tert-butyldiphenylsilyl-2-deoxy-4-O-(2-naphthylmethyl)-α-D-glucopyranosyl trichloroacetimidate 
• 1314746-13-8 1,6-anhydro-4-O-[2-azido-3-O-(4-bromobenzyl)-6-O-tert-butyldiphenylsilyl-2-deoxy-4-O-(2-naphthylmethyl)-α-D-glucopyranosyl]-2-O-benzoyl-3-O-benzyl-β-L-idopyranose 
• 1314746-20-7 p-methylphenyl 2-azido-2-deoxy-4-O-(2-naphthylmethyl)-1-thio-D-glucopyranoside ⁽⁴⁾ 
• 1314746-19-4 C₂₂H₄₁N₃O₄SSi₃ 
• 1314746-14-9 p-methylphenyl 2-azido-3-O-(p-bromobenzyl)-6-O-tert-butyldiphenylsilyl-2-deoxy-4-O-(2-naphthylmethyl)-1-thio-D-glucopyranoside 

Downstream Products

• 1314746-46-7 C₇₆H₈₂BrN₃O₁₈Si 
• 1314746-24-1 C₅₈H₆₄BrN₃O₁₅Si 
• 1314746-10-5 C₅₈H₆₂BrCl₃N₄O₁₄Si 
• 1314746-23-0 C₅₄H₅₈BrN₃O₁₂Si 
• 1374561-92-8 [2-azido-3-O-(4-bromobenzyl)-6-O-tert-butyldiphenylsilyl-2-deoxy-4-O-(2-naphthylmethyl)-α-D-glucopyranosyl]-(1->4)-(6-O-acetyl-2-O-benzoyl-3-O-benzyl-α-L-idopyranosyl)-(1->4)-[2-azido-3-O-(4-bromobenzyl)-6-O-tert-butyldiphenylsilyl-2-deoxy-α-D-glucopyranosyl]-(1->4)-1,6-anhydro-2-O-benzoyl-3-O-benzyl-β-L-idopyranose 

Relevant academic research and scientific papers

Trisaccharide Sulfate and Its Sulfonamide as an Effective Substrate and Inhibitor of Human Endo- O-sulfatase-1

Human endo-O-sulfatases (Sulf-1 and Sulf-2) are extracellular heparan sulfate proteoglycan (HSPG)-specific 6-O-endosulfatases, which regulate a multitude of cell-signaling events through heparan sulfate (HS)-protein interactions and are associated with th

α-glycosylation by d -glucosamine-derived donors: Synthesis of heparosan and heparin analogues that interact with mycobacterial heparin-binding hemagglutinin

Numerous biomolecules possess α-d-glucosamine as structural component. However, chemical glycosylations aimed at this backbone are usually not easily attained without generating the unwanted β-isomer. We report herein a versatile approach in affording full α-stereoselectivity built upon a carefully selected set of orthogonal protecting groups on a d-glucosaminyl donor. The excellent stereoselectivity provided by the protecting group combination was found independent of leaving groups and activators. With the trichloroacetimidate as the optimum donor leaving group, core skeletons of glycosylphosphatidyl inositol anchors, heparosan, heparan sulfate, and heparin were efficiently assembled. The orthogonal protecting groups were successfully manipulated to further carry out the total syntheses of heparosan tri- and pentasaccharides and heparin di-, tetra-, hexa-, and octasaccharide analogues. Using the heparin analogues, heparin-binding hemagglutinin, a virulence factor of Mycobacterium tuberculosis, was found to bind at least six sugar units with the interaction notably being entropically driven.

Synthesis of 3-O-sulfonated heparan sulfate octasaccharides that inhibit the herpes simplex virus type 1 host-cell interaction

Cell surface carbohydrates play significant roles in a number of biologically important processes. Heparan sulfate, for instance, is a ubiquitously distributed polysulfated polysaccharide that is involved, among other things, in the initial step of herpes simplex virus type 1 (HSV-1) infection. The virus interacts with cell-surface heparan sulfate to facilitate host-cell attachment and entry. 3-O-Sulfonated heparan sulfate has been found to function as an HSV-1 entry receptor. Achieving a complete understanding of these interactions requires the chemical synthesis of such oligosaccharides, but this remains challenging. Here, we present a convenient approach for the synthesis of two irregular 3-O-sulfonated heparan sulfate octasaccharides, making use of a key disaccharide intermediate to acquire different building blocks for the oligosaccharide chain assembly. Despite substantial structural differences, the prepared 3-O-sulfonated sugars blocked viral infection in a dosage-dependent manner with remarkable similarity to one another.