Artificial synthetic receptors as regulators of protein activity.

Som Dutt, Constanze Wilch, Thomas Schrader

Department of Chemistry, University of Duisburg-Essen, Universitätsstr. 7, 45117 Essen, Germany.

Chemical communications (Cambridge, England) 2011 May 21

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This article discusses most recent work and progress in the direction of a rational design of small molecule receptors that efficiently interfere with the biological function of a particular receptor or enzyme-some of which are therapeutically relevant. More specifically, the following topics are highlighted here: the inhibition of voltage-dependent potassium channels of the K(v)1.x family by designed porphyrin and calix[4]arene ligands, the structural and functional recovery of the tetramerization domain of mutated P53 protein by tailored calix[4]arene ligands and the control over LDH activity by supramolecular signaling. Finally a new way to modulate NAD(+)-dependent enzymatic activities by molecular clips and tweezers is presented. © The Royal Society of Chemistry 2011

Citation

Som Dutt, Constanze Wilch, Thomas Schrader. Artificial synthetic receptors as regulators of protein activity. Chemical communications (Cambridge, England). 2011 May 21;47(19):5376-83