147157-96-8Relevant academic research and scientific papers
Solid-phase synthesis of thioether-linked glycopeptide mimics for application to glycoprotein semisynthesis.
Macmillan, Derek,Daines, Alison M,Bayrhuber, Monika,Flitsch, Sabine L
, p. 1467 - 1470 (2007/10/03)
[reaction: see text]. Glycoproteins are particularly suited to protein semisynthesis since homogeneous samples for biological analyses are not readily available using traditional recombinant techniques. Here we apply glycosyl iodoacetamides, normally used for the modification of bacterially derived proteins, to solid-phase glycopeptide synthesis. This provides access to glycopeptide alpha-thioesters, which may lend themselves to the semisynthesis of homogeneous N-linked glycoprotein mimics and novel glycopeptide libraries.
Stereoselective Synthesis of Glycosides and Anomeric Azides of Glucosamine
Unverzagt, Carlo,Kunz, Horst
, p. 570 - 578 (2007/10/02)
The β-azide of O-acetyl protected N-acetyl glucosamine is efficiently accessible via a phase-transfer-catalyzed reaction of the corresponding glycosyl chloride with sodium azide.The azido group revealed to be a useful anomeric protection for modifications of the protecting group pattern of the glucosamine unit.Exchange of the O-acyl groups by 4-methoxybenzylidene and 4-methoxybenzyl (Mpm) protection delivered regioselectively blocked glucosaminyl azide derivatives.In contrast, the N-phthaloyl protected glucosaminyl azide was obtained quantitatively from the corresponding glycosyl fluoride via a boron trifluoride-promoted reaction with trimethylsilyl azide.N-Phthaloyl glucosaminyl fluoride was also revealed to be useful in the synthesis of β-glucosamine glycosides and saccharides.Chitobiosyl azide 21 carrying a selectively removable 6-O-Mpm protection was synthesized from the O-acetyl protected N-phthaloyl glucosaminyl bromide and N-acetylglucosaminyl azide 13 as an acceptor selectively deblocked at O-4.
