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. 2010 Apr 17;66(16):2907-2918.
doi: 10.1016/j.tet.2010.02.015.

Chemical Sulfation of Small Molecules - Advances and Challenges

Rami A Al-Horani  1 , Umesh R Desai
Affiliations

Chemical Sulfation of Small Molecules - Advances and Challenges

Rami A Al-Horani et al. Tetrahedron. .
No abstract available

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Figures

Figure 1
Figure 1. Structures of endogeneous sulfated ligands shown to be involved in generating specific physiological or pathological responses
Sulfate groups highlighted in blue (Sialyl Lewis X and DEFGH) are known to be essential for interaction with target proteins. Such sulfate groups have not been rigorously identified for glycoprotein D octasaccharide.
Figure 2
Figure 2. Interaction of sulfate group(s) with positively charged nitrogen containing groups
A) The interaction relies solely on the ionic charges on the two groups. This interaction is defined as Coulomb-type interaction and occurs over a longer range in comparison to other atomic interactions. It is isotropic and does not involve any geometrical constraints. B) The interaction between a Lys or an Arg with one or more sulfate groups may sandwich an H atom resulting in the formation of a hydrogen bond. This H-bond may not be linear, yet provides sufficient energy to engineer specificity of recognition. The stoichiometry of interaction here may be 1:1 or 1:2 per nitrogen atom. C) For arginine, a linear H-bond geometry is feasible generating significant bond energy and greater specificity of recognition. The stoichiometry of interaction here is 1:1. Geometry C) is expected to be most stable.
Figure 3
Figure 3. Close-up view of the heparin-binding site in antithrombin
The structure of co-complex was obtained from PDB (filename ‘1e03’). Green ribbon shows antithrombin and magenta represents the heparin-binding site. Pentasaccharide DEFGH is shown in ball-and-stick representation. Extensive interactions between antithrombin arginine and lysines with multiple sulfate groups of DEFGH engineer the high affinity, high specificity interaction. Majority of the non-ionic binding energy involved in the heparin – antithrombin interaction is thought to arise from the hydrogen bond type interaction with sulfate groups. Figure modified from Desai UR. Med. Res. Rev. 2004; 24:151–181).
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