The design, synthesis and preliminary conformational studies of two polypeptides exhibiting ß a ß type folding topologies are presented. In the design of the model peptides the general concept for the construction of new proteins developed in the preceeding paper was applied. According to this strategy, amphiphilic helices and ß-sheets are linked together via hydrophilic loops to attain three-dimensional structures of higher order ( ‘supersecondary structures'). Com puter-assisted molecular modelling served as a valuable tool for minimizing conformational con straints within the molecules. The 38-residue peptide MI was synthesized using polyethylene glycol (PEG) as solubilizing polymeric support ( ‘Liquid-Phase synthesis’). Conformationally in duced changes in the physico-chemical properties of the growing peptide chain stressed the significance of conformational effects in peptide synthesis reported earlier. Similar observations were made during the solid-phase synthesis of the 35-peptide MIL CD and IR spectroscopic studies revealed a high degree o f secondary structure for both folding units. The present data strongly support the adoption of a three-dimensional structure for both models.