title: Signal transduction in oligoamide foldamers by selective non-covalent binding of chiral phosphates at a urea binding site.
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 active13C labels. The remote induction of screw sense preference indicates successful communication of a signal originating solely from non-covalent binding.
authors.affiliation: School of Chemistry, University of Bristol, Cantock's Close, Bristol BS8 1TS, UK. j.clayden@bristol.ac.uk.
authors.forename: Katharina
authors.initials: K
authors.lastname: Gratzer
authors.forename: Vincent
authors.initials: V
authors.lastname: Diemer
authors.forename: Jonathan
authors.initials: J
authors.lastname: Clayden
mesh_terms: D001665:Binding Sites; D009757:Nylons / Q000737:chemistry*; D010710:Phosphates / Q000737:chemistry*; D015398:Signal Transduction; D013237:Stereoisomerism; D013379:Substrate Specificity; D014508:Urea / Q000737:chemistry*
chemical_list: D009757:Nylons; D010710:Phosphates; D014508:Urea