The ability to design foldamers that mimic the defined structural motifs of natural biopolymers is critical for the continued development of functional biomimetic molecules. We have found that simple, peptoid monomer model systems allow for the effective isolation of individual interactions within the peptoid backbone and side chains and can facilitate the study of the role of these interactions in restricting local peptoid conformation. Herein, we present an analysis of a set of peptoid monomers and an oligomer containing N-aryl side chains capable of hydrogen bonding with the peptoid backbone.

Arrays of stilbenes have been prepared in high purity by using Heck reactions on planar cellulose support, and demonstrate the compatibility of the small molecule macroarray platform with metal-mediated reactions for the first time. Biological screening of the stilbene library revealed several compounds with the ability to inhibit quorum sensing responses in bacteria, expanding the activity of this compound class.