Signal transduction in oligoamide foldamers by selective non-covalent binding of chiral phosphates at a urea binding site

Org Biomol Chem. 2017 May 3;15(17):3585-3589. doi: 10.1039/c7ob00660h.

Abstract

The transduction of biological signals depends on the spatial communication of conformational change. We report a synthetic mimic of this signal transduction process in which non-covalent binding induces a change in the position of equilibrium between two rapidly interconverting screw-sense conformers of a synthetic helical polyamide. Selectivity was achieved by incorporating at the N-terminus of the polyamide a urea-based anion recognition site capable of binding chiral phosphate anions. As a result of solvent-dependent binding, an induced conformational change propagates from the binding site through the amide chain, leading to a screw-sense preference detectable in the form of a chemical shift separation between two NMR active 13C labels. The remote induction of screw sense preference indicates successful communication of a signal originating solely from non-covalent binding.

MeSH terms

  • Binding Sites
  • Nylons / chemistry*
  • Phosphates / chemistry*
  • Signal Transduction
  • Stereoisomerism
  • Substrate Specificity
  • Urea / chemistry*

Substances

  • Nylons
  • Phosphates
  • Urea