Extended Sulfo-Pillar[6]arenes ─ a New Host Family and Its Application in the Binding of Direct Oral Anticoagulants.

Herein, we report the synthesis of extended sulfo-pillar[6]arenes (), a new host class with a pedigree in salt tolerance and ultrahigh binding affinity toward multiple drug classes. The parent sulfo-pillar[6]arene is a high-affinity host with the potential to act as a supramolecular reversal agent. However, it lacks synthetic diversification of the core scaffold.

Molecular recognition of methylated amino acids and peptides by Pillar[6]MaxQ.

We report the molecular recognition properties of Pillar[]MaxQ (P[]MQ) toward a series of (methylated) amino acids, amino acid amides, and post-translationally modified peptides by a combination of H NMR, isothermal titration calorimetry, indicator displacement assays, and molecular dynamics simulations. We find that P6MQ is a potent receptor for -methylated amino acid side chains. P6MQ recognized the H3K4Me peptide with = 16 nM in phosphate buffered saline.

Polycomb Paralog Chromodomain Inhibitors Active against Both CBX6 and CBX8*.

Methyllysine reader proteins bind to methylated lysine residues and alter gene transcription by changing either the compaction state of chromatin or by the recruitment of other multiprotein complexes. The polycomb paralog family of methyllysine readers bind to trimethylated lysine on the tail of histone 3 (H3) via a highly conserved aromatic cage located in their chromodomains. Each of the polycomb paralogs are implicated in several disease states.

Pan-specific and partially selective dye-labeled peptidic inhibitors of the polycomb paralog proteins.

Epigenetic regulation of gene expression is in part controlled by post-translational modifications on histone proteins. Histone methylation is a key epigenetic mark that controls gene transcription and repression. There are five human polycomb paralog proteins (Cbx2/4/6/7/8) that use their chromodomains to recognize trimethylated lysine 27 on histone 3 (H3K27me3).