Methyl 2,3-di-O-acetyl-4-O-levulinoyl-1-O-(2,2,2-trichloro-2-iminoethyl)-L-idopyranosiduronate

Abstract

In the title compound, C 18 H 22 Cl 3 NO 11 , a novel derivative of lidopyranosiduronic acid, the six-membered ring adopts a chair conformation.

Crystal Polymorphism of Methyl 2,3,4-tri-O-acetyl-1-O-(trichloroacetimidoyl)-α-d-glucopyranouronate

“…Atomic numbering for all molecules of compound 1 is shown in Fig 3 and (Table 2). This latter motif is similar to that reported in the crystal structure of methyl 2,3-di- [17]. By contrast, Form ІІ is characterised by the absence of hydrogen bonds when forming the crystal lattice.…”

Sulfation Effects of Chondroitin Sulfate to Bind a Chemokine in Aqueous Medium: Conformational Heterogeneity and Dynamics from Molecular Simulation

“…16−18 Nuclear magnetic resonance (NMR) investigation reported that the processes of binding and recognitions are sometimes governed through the nonchair forms, e.g., the L-iduronic residues of the anticoagulant GAG can activate the antithrombin III by adopting the skew-boat 2 S O ring conformer. 19 Among GAGs, the most prevalent GAGs are chondroitin sulfate (CS) and heparan sulfate (HS), and their major target proteins are chemokines, axon guidance molecules, cell-surface receptors, and growth factors. 14,20,21 While most attention has been paid to various HS−protein interactions, much less has been given to CS.…”

“…The epimerization and sulfation add massive heterogeneity and distinct topologies in the GAG population, which further affects human health and disorders. − In this context, sulfation is a dynamic and complex post-translational modification process occurring at various positions within the backbone of GAGs and modulates extracellular signal . GAG conformational flexibilities, to some extent, additionally arise from the distortion of the pyranose rings associated with the ring pucker. − Nuclear magnetic resonance (NMR) investigation reported that the processes of binding and recognitions are sometimes governed through the nonchair forms, e.g., the l -iduronic residues of the anticoagulant GAG can activate the antithrombin III by adopting the skew-boat 2 S O ring conformer . Among GAGs, the most prevalent GAGs are chondroitin sulfate (CS) and heparan sulfate (HS), and their major target proteins are chemokines, axon guidance molecules, cell-surface receptors, and growth factors. ,, While most attention has been paid to various HS–protein interactions, much less has been given to CS.…”