Lysine and arginine methylation are two common post-translational modifications in proteins that trigger complex signaling events that control gene expression.  Because dysregulation of Lys and Arg methylation plays a role in many types of cancer, there is a need for new tools for sensing these modifications.  To this end, we are utilizing dynamic combinatorial chemistry to identify new synthetic receptors for the different methylation states of Lys and Arg.  Through structure-function studies and iterative redesign, we have developed a set of synthetic receptors which differential selectivity for these modified amino acids.  Our studies have shown that small changes in the structures of the building blocks can have substantial impact on the selectivity of the receptors, and iterative redesign can significantly improve binding affinity.  These receptors are being developed as sensors for histone protein modifications.  Results of these studies will be presented.<br/>

From host-guest chemistry to the nucleosome: Studies in biomolecular recognition

249th National Meeting (2015)

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