Design and synthesis of an alpha-helical peptide containing periodic proline residues

A thirty-residue peptide (PERI COIL-1) has been designed with a new type of alpha-helical structure, which is capable of folding into an amphiphilic helix bending at 4 periodic prolines in the sequence. Two such helices should form a dimer by supercoiling about one another in an antiparallel direction in the design. With this arrangement, close packing between them is maintained through the hydrophobic interaction pattern called 'leucine zipper'. PERI COIL-1 has been obtained by solid-phase peptide synthesis, and characterized by circular dichroic spectroscopy, sedimentation equilibrium experiments and NMR. The result of the analyses shows that it preferentially forms a helical tetramer in aqueous solution.