4704-15-8Relevant articles and documents
The structure of the glycolipid components of the aridicin antibiotic complex
Jeffs,Chan,Sitrin,et al.
, p. 1726 - 1731 (1985)
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Regioselective sulfamoylation at low temperature enables concise syntheses of putative small molecule inhibitors of sulfatases
Miller, Duncan C.,Carbain, Benoit,Beale, Gary S.,Alhasan, Sari F.,Reeves, Helen L.,Baisch, Ulrich,Newell, David R.,Golding, Bernard T.,Griffin, Roger J.
supporting information, p. 5279 - 5284 (2015/05/13)
Regioselective sulfamoylation of primary hydroxyl groups enabled a 5-step synthesis (overall yield 17%) of the first reported small molecule inhibitor of sulfatase-1 and 2, ((2S,3R,4R,5S,6R)-4,5-dihydroxy-2-methoxy-6-((sulfamoyloxy)methyl)tetrahydro-2H-pyran-3-yl)sulfamic acid, which obviated the use of hydroxyl protecting groups and is a marked improvement on the reported 9-step synthesis (overall yield 9%) employing hazardous trifluoromethylsulfonyl azide. The sulfamoylation methodology was used to prepare a range of derivatives of 1, and inhibition data was generated for Sulf-2, ARSA and ARSB.
Hybrid aminoglycoside antibiotics via tsuji palladium-catalyzed allylic deoxygenation
Hanessian, Stephen,Maianti, Juan Pablo,Matias, Rowena D.,Feeney, Lee Ann,Armstrong, Eliana S.
supporting information; experimental part, p. 6476 - 6479 (2012/02/14)
Biosynthetically inspired manipulation of the antibiotic paromomycin led, in six high-yielding steps, to a ring A harboring an R,β-unsaturated 6′- aldehyde and an allylic 3′-methylcarbonate group. Tsuji deoxygenation in the presence of 5 mol % Pd2(dba)3 and Bu3P granted access to a novel series of 3′,4′-dideoxy- 4′,5′-dehydro ring A hybrids. The neomycin-sisomicin hybrid exhibited superior in vitro antibacterial activity to the parent compound neomycin.
Synthesis of heparin partial structures and their binding activities to platelets
Koshida, Shuhei,Suda, Yasuo,Sobel, Michael,Ormsby, Julie,Kusumoto, Shoichi
, p. 3127 - 3132 (2007/10/03)
A synthetic pentasaccharide corresponding to the antithrombin III-binding region in heparin was also found to bind to human platelets. To identify the platelet-binding site in the pentasaccharide which is expected to be a novel sequence in heparin responsible for its platelet-binding, five partial structures of this particular pentasaccharide were synthesized. In a competitive assay using [3H]-heparin, a trisaccharide, O-(2-deoxy-2-sulfamido-3,6-di-O-sulfo-α-D-glucopyranosyl)- (1→4)-O-(2-O-sulfo-α-L-idopyranosyluronic acid)-(1→4)-2-deoxy-2-sulfamido-6-O-sulfo-α-D-glucopyranose, was concluded to be a high-affinity site for heparin's binding to platelets.
