677031-67-3

Upstream product

• 1887-29-2 sodium phenylthiosulfonate 
• 572-09-8 2,3,4,6-tetra-O-acetyl-α-D-glucopyranosyl bromide 
• 873-55-2 sodium benzenesulfonate 

Downstream Products

• 1028450-55-6 C₃₀H₄₇N₃O₁₅S₂ 
• 1028450-40-9 C₂₀H₂₉NO₁₂S₂ 
• 1028450-42-1 C₁₉H₂₈N₂O₁₁S₂ 

Relevant academic research and scientific papers

One-pot synthesis of glycosyl phenylthiosulfonates from sulfinate, S and glycosyl bromides

Glycosyl phenylthiosulfonates are reagents which are valuable for the S-glycosylation decoration of organic compounds and proteins. Here, one-pot multiple-component synthesis of glycosyl phenylthiosulfonates from sulfinate, sulfur powder and glycosyl bromides is reported. The reactions afford glycosyl phenylthiosulfonates in good yields under mild conditions. Further application and exploration of glycosyl phenylthiosulfonates are still on underway in our group.

From disulfide- to thioether-linked glycoproteins

(Chemical Presented) Strengthening the bond: The introduction of a thiol tag in combination with chemoselective ligation to form a disulfide-linked bioconjugate is a selective and useful method for site-selective protein glycosylation. The phosphine-mediated desulfurization of such glycoconjugates to their reductant-resistant thioether-linked counterparts completes a convergent, site-selective synthesis of thioether-linked glycoproteins (see scheme).

REAGENTS AND METHODS FOR THE FORMATION OF DISULFIDE BONDS AND THE GLYCOSYLATION OF PROTEINS

Methods and reagents for the formation of disulfide bonds, particularly in proteins, peptides and amino acids. The methods and reagents are particularly useful for the controlled glycosylation of proteins, peptides and amino acids. The methods utilise thiosulfonate or selenenylsulfide compounds as reagents or intermediates. Some proteins and peptides comprising selenenylsulfide groups also form part of the invention.

Glycosyl phenylthiosulfonates (glyco-PTS): novel reagents for glycoprotein synthesis.

Controlled site-selective glycosylation can be achieved by combining site-directed cysteine mutagenesis with chemical modification of the introduced thiol; a new class of more efficient chemoselective reagents, glycosyl phenylthiosulfonates, allow rapid glycosylations of representative simple thiols, peptides and proteins.