678968-47-3

Upstream product

• 1666-13-3 diphenyl diselenide 
• 3068-32-4 1-bromo-1-deoxy-2,3,4,6-tetra-O-acetyl-a-D-galactopyranoside 
• 252665-94-4 bis(2,3,4,6-tetra-O-acetyl-1-deoxy-1-thio-β-D-galactopyranosyl)-1,1'-disulfide 
• 75801-94-4 tetra-O-acetyl-α-iodogalactopyranose 
• 4163-60-4 β-D-galactose peracetate 
• 40591-65-9 2,3,4,6-tetra-O-acetylgalactopyranosyl-1-β-pseudothiourea hydrobromide 

Downstream Products

• 1192362-59-6 5,6-diacetoxyindol-3-yl 2,3,4,6-tetra-O-acetyl-1-thio-β-D-galactopyranoside 
• 1666-13-3 diphenyl diselenide 
• 252665-94-4 bis(2,3,4,6-tetra-O-acetyl-1-deoxy-1-thio-β-D-galactopyranosyl)-1,1'-disulfide 

Relevant academic research and scientific papers

A straightforward synthetic access to symmetrical glycosyl disulfides and biological evaluation thereof

Symmetrical glycosyl disulfides can be prepared within a few hours from per-O-acetylated precursors via a sequential approach entailing short reactions and no purification of any intermediate. The final thiolate-to-disulfide oxidation step is noticeably accelerated by low amounts of phenyl diselenide under air. Applicability of the strategy to non-saccharidic symmetrical alkyl disulfides has also been examined. A preliminary assay of the cytotoxic activity of symmetrical 1,1′- disulfides was performed on two human tumor cell lines, and a noteworthy activity was recorded for a range of these synthetic compounds.

Synthesis of mixed glycosyl disulfides/selenenylsulfides using benzyltriethylammonium tetrathiomolybdate as a sulfur transfer reagent

An easy and mild method has been developed for the synthesis of mixed glycosyl disulfides/selenenylsulfides from glycosyl halides and diaryl/dialkyl dichalcogenides in the presence of benzyltriethylammonium tetrathiomolybdate [(BnEt3N)2MoS4]. The salient feature of this method is the sulfur transfer from [BnEt3N]2MoS4 to form glycosyl disulfides which with excess tetrathiomolybdate further undergo exchange reaction with other dichalcogenides in a one-pot operation.

Glycosylated eumelanin building blocks by thioglycosylation of 5,6-diacetoxyindole with an expedient selenium-based dynamic-mixture methodology

A series of 3-thioglycosylated 5,6-diacetoxyindole derivatives, which are important tools for eumelanin research and application, were prepared through a practical and efficient approach exploiting a dynamic mixture of thioglycoside agents. The strategy is feasible for installing both mono- and disaccharide units and relies on the facile in situ conversion of glycosyl disulfides into the corresponding, more reactive, phenylselenenyl sulfides in the presence of diphenyl diselenide, N-bromosuccinimide (NBS) and tetrabutylammonium bromide (TBAB). An expedient thioglycosidation of 5,6-diacetoxyindole with a dynamic mixture of thioglycosides is described. Copyright

Disentangling Eumelanin "black chromophore": Visible absorption changes as signatures of oxidation state- and aggregation-dependent dynamic interactions in a model water-soluble 5,6-dihydroxyindole polymer

A fundamental unsettled issue concerning eumelanins, the functional biopolymers of human skin and hair, is why they are black. The experimental difficulty lies in the virtual insolubility of these pigments, causing marked scattering effects and hindering

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.

Glyco-SeS: Selenenylsulfide-mediated protein glycoconjugation - A new strategy in post-translational modification

Site-selective glycosylation by Se-S-mediated ligation has led to the efficient formation of a wide variety of conjugates 1 without the need for a large excess of the carbohydrate reagent. By this convergent method it was possible to introduce a heptasaccharide glycan selectively, and to perform a multiple site-selective chemical glycosylation of protein. A chemically Cysglycosylated glycoprotein was elaborated enzymatically.