Glycosaminoglycans (GAGs), linear sulfated oligosac-ESI-MS analyses to ascertain the number and structures of the library members. The combinatorial protocol involves charides, are involved in numerous biological events ranging from tissue structure to protein activity regulation. The sulfatation/group manipulation sequences which rely on the fact that, although previously reported to be labile groups, combinatorial nature of their oligosaccharidic framework and sulfatation pattern (sulfoforms) prompted us to develop a sulfate esters withstand many classical reactions used in molecular glycochemistry. Thus, we used sulfate groups as combinatorial approach toward the synthesis of GAG fragments. Using a liquid-phase split and pool protocol, the efficient hydroxyl protecting groups in a combinatorial glucosyl to glucuronyl oxidation sequence involving a Swern eight basic chondroitin sulfate (CS) disaccharides have been prepared from a key CS disaccharide scaffold bearing oxidation, followed by direct conversion of the aldehyde to the methyl ester. Split and pool methodology is thus shown orthogonal protecting groups. This approach saves 25 steps compared to a multi-parallel synthesis. We chose to prepare to be a powerful tool in gaining access to molecular diversity in GAGs and in the preparation of sulfoforms of a given restricted libraries, but with a high structural confidence. Each step was followed by HPLC, 1 H-and 13 C-NMR, and oligosaccharide.
dehydromannosyl residue at the reducing end.