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Design and synthesis of an α‐helical peptide containing periodic proline residues
Author(s) -
Kitakuni Eiichi,
Horiuchi Tokio,
Oda Yasushi,
Oobatake Motohisa,
Nakamura Haruki,
Tanaka Toshiki
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80065-o
Subject(s) - antiparallel (mathematics) , tetramer , crystallography , coiled coil , peptide , circular dichroism , dimer , chemistry , sedimentation equilibrium , trimer , folding (dsp implementation) , helix (gastropod) , leucine zipper , nuclear magnetic resonance spectroscopy , peptide conformation , heptad repeat , stereochemistry , peptide sequence , biochemistry , physics , ecology , organic chemistry , quantum mechanics , snail , magnetic field , gene , electrical engineering , biology , enzyme , engineering
A thirty‐residue peptide (PERI COIL‐1) has been designed with a new type of α‐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.