7531-49-9Relevant academic research and scientific papers
NOVEL ANTI-INFLAMMATORY PRO-DRUGS
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Page/Page column 31-32, (2009/01/24)
The present invention relates to compounds according to formula (I): wherein R is selected from the group consisting of anti-inflammatory agents and pharmaceutically acceptable salts thereof, pharmaceutical compositions comprising compounds of formula (I) and the use of these pharmaceutical compositions for the treatment or prophylaxis of chronic inflammatory diseases, in particular those that are caused by chronically activated macrophages. The chronic inflammatory disease is in particular atherosclerosis, (rheumatoid) arthritis, an (auto)immune disease or sarcoidosis.
The (2-Phenyl-2-trimethylsilyl)ethyl-(PTMSEL)-Linker in the Synthesis of Glycopeptide Partial Structures of Complex Cell Surface Glycoproteins
Wagner, Michael,Dziadek, Sebastian,Kunz, Horst
, p. 6018 - 6030 (2007/10/03)
The (2-phenyl-2-trimethylsilyl)ethyl-(PTMSEL) linker represents a novel fluoride-sensitive anchor for the solid-phase synthesis of protected peptides and glycopeptides. Its cleavage is achieved under almost neutral conditions using tetrabutylammonium fluo
Probing the mechanism of a fungal glycosyltransferase essential for cell wall biosynthesis. UDP-Chitobiose is not a substrate for chitin synthase
Chang, Robert,Yeager, Adam R.,Finney, Nathaniel S.
, p. 39 - 41 (2007/10/03)
Chitin synthase is responsible for the biosynthesis of chitin, an essential component of the fungal cell wall. There is a long-standing question as to whether "processive" transferases such as chitin synthase operate in the same manner as non-processive transferases. The question arises from analysis of the polysaccharide structure - in chitin, for instance, each sugar residue is rotated ca. 180 deg relative to the preceding sugar in the chain. This requires that the enzyme account for the alternating "up/down" configuration during biosynthesis. An enzyme with a single active site, analogous to the non-processive transferases - would have to accommodate a distorted glycosidic linkage at every other synthetic step. An alternative proposal is that the enzyme might assemble the disaccharide donor, addressing the "up/down" conformational problem prior to polymer synthesis. We present compelling evidence that this latter hypothesis is incorrect.
Enzyme-Catalyzed Glycosylation of Peptides Using a Synthetic Lipid Disaccharide Substrate
Lee, Jung,Coward, James K.
, p. 4126 - 4135 (2007/10/02)
A lipid disaccharide, consisting of chitobiose linked to dolichol via an α-1-pyrophosphate, has been synthesized for use as a substrate in the enzyme-catalyzed glycosylation of peptides.For the purpose of confirming the structure of the reaction product,
Synthesis of Partial Structures of N-Glycopeptides Representing the Linkage Regions of the Transmembrane Neuraminidase of an Influenca Virus and of Factor B of the Human Complement System
Kunz, Horst,Waldmann, Herbert,Maerz, Joachim
, p. 45 - 50 (2007/10/02)
The synthesis of the protected N-chitobiosylasparaganine peptides 12a and 14, which correspond to the linkage regions of factor B of the human complement system and of the transmembrane neuraminidase of an influenza virus, was accomplished by applying the protecting group combination Boc group/allyl ester together with acetyl groups in the carbohydrate part.From 12a the allyl ester and the acetates were simultaneously removed using ammonia in methanol.The Boc group was cleaved without side reactions using anhydrous trifluoroacetic acid.Attempts to remove the Boc-protecting group from the glycopeptides already deblocked in the carbohydrate part resulted predominantly in the cleavage of the O-glycosidic bond.
