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

Abstract

We report the molecular recognition properties of Pillar[n]MaxQ (P[n]MQ) toward a series of (methylated) amino acids, amino acid amides, and post-translationally modified peptides by a combination of ¹H NMR, isothermal titration calorimetry, indicator displacement assays, and molecular dynamics simulations. We find that P6MQ is a potent receptor for N-methylated amino acid side chains. P6MQ recognized the H3K4Me₃ peptide with K_d = 16 nM in phosphate buffered saline.