Gao, Chao published the artcileUnique Binding Specificities of Proteins toward Isomeric Asparagine-Linked Glycans, Synthetic Route of 59-23-4, the main research area is asparagine Nglycan Siglec protein structure influenza virus infection; N-glycan isomer; N-glycan-binding specificity; chemoenzymatic synthesis; glycan-binding proteins; glycosyltransferases; microarray.
The glycan ligands recognized by Siglecs, influenza viruses, and galectins, as well as many plant lectins, are not well defined. To explore their binding to asparagine (Asn)-linked N-glycans, we synthesized a library of isomeric multiantennary N-glycans that vary in terminal non-reducing sialic acid, galactose, and N-acetylglucosamine residues, as well as core fucose. We identified specific recognition of N-glycans by several plant lectins, human galectins, influenza viruses, and Siglecs, and explored the influence of sialic acid linkages and branching of the N-glycans. These results show the unique recognition of complex-type N-glycans by a wide variety of glycan-binding proteins and their abilities to distinguish isomeric structures, which provides new insights into the biol. roles of these proteins and the uses of lectins in biol. applications to identify glycans.
Cell Chemical Biology published new progress about Agglutinins Role: BSU (Biological Study, Unclassified), BIOL (Biological Study). 59-23-4 belongs to class alcohols-buliding-blocks, name is (2R,3S,4S,5R)-2,3,4,5,6-Pentahydroxyhexanal, and the molecular formula is C6H12O6, Synthetic Route of 59-23-4.
Referemce:
Alcohol – Wikipedia,
Alcohols – Chemistry LibreTexts