Investigating the effects of structure on sulfate recognition by neutral dipeptide receptors

A small library of neutral peptide-based anion receptors was synthesised, where changes were made to the scaffold structure to investigate the effect these structural features have on the anion binding ability of these receptors. These changes included shortening the peptide side chain lengths, increasing the number of electron withdrawing substituents present on the squaramide phenyl substituents and increasing the length and flexibility of the peptide backbone. An effort was also made to increase the aqueous solubility of these receptors by functionalising the N -terminus of the peptide with a hydrophilic moiety. All the receptors displayed strong affinity and selectivity for sulfate in 20% v / v H 2 O/DMSO- d 6 and a 5-fold increase in the affinity of the thiourea receptors was observed upon shortening the side chains by one methylene unit. Overall, the squaramide derivatives displayed much stronger association, in this competitive media, than the thiourea based receptors.