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Evidently, the MIP approach leads to selectivity factors of about 3, whereas the ligand system prefers WGA by a factor of more than 7.
This leads to selectivity within the Plk family and towards Aurora A. This selectivity can be explained by docking studies of SBE13 into the binding pocket of homology models of Plk1, Plk2 and Plk3 in their inactive conformation.
The primary sulfonamide moiety is a better zinc-binding group in the design of CAIs as compared to the carboxylate/hydroxamate one, but the presence of hydroxamate functionalities in the molecule of CAIs leads to selectivity for the tumor-associated isozyme IX over the ubiquitous, cytosolic isoform II.
That means many contact sites between binding pocket and ligand, which in turn leads to selectivity for the shape of the ligand.
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The structural differences confirmed to lead to selectivity can be utilized in the design of new subtype-selective A1R or A2AR antagonists.
Optimized molecularly imprinted sensor layers lead to selectivity factors of at least 2 compared to other bivalent ions.
However, the ways that accessory binding sites lead to selectivity for specific classes of oligosaccharide ligands continue to be elucidated.
Computational studies on a model system have allowed the structural parameters that lead to selectivity in these reaction processes to be analysed.
A high Si/Al ratio leads to high selectivity but low catalyst activity; Both MgO modification and phosphorus modification increase the selectivity to 4,4′-DMBP, but less than 80%.
This often leads to increased selectivity towards large cations.
On the other hand, the less active foam catalyst leads to higher selectivity.
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