The privileged role of β-turn secondary structures in molecular recognition impels synthesis of rigid surrogates to study structure-activity relationships in peptide-based drug discovery. We have previously reported effective methods for introducing linear semicarbazide residues into azapeptides to prepare mimics of type I and II’ β-turns [1]. Solid-phase chemistry for the synthesis and Diels-Alder reaction of Fmoc-protected azopeptides has now been developed and used to construct aza-pipecolyl (azaPip) peptides to favor cis-amide isomer geometry and type VI β-turn conformation in peptides [2]. Moreover, solid-phase methods for modifying N-amino-imidazalone (Nai) residues has been developed to prepare mimics of both turn backbone geometry and side chain function [3]. The solid-phase synthesis of azaPip- and Nai-peptides will be presented and used to study ligands of opioid and cluster of differentiation-36 receptors in programs targeted to treat pain and inflammation.