Chirality organization of ferrocenes bearing dipeptide chains of heterochiral sequence.
[structures: see text] The symmetrical introduction of two dipeptide chains of heterochiral sequence (-L-Ala-D-Pro-NHPy) into the ferrocene scaffold as a central reverse-turn unit was demonstrated to induce both antiparallel beta-sheet-like and type II beta-turn-like structures simultaneously, affording the chirality-organized structure. The ferrocene bearing only one dipeptide chain (-L-Ala-D-Pro-NHPy) exhibited a left-handed helically ordered molecular assembly through a network of intermolecular hydrogen bonds instead of intramolecular hydrogen bonds.
Moriuchi
Toshiyuki
T
Department of Applied Chemistry, Graduate School of Engineering, Osaka University, Yamada-oka, Suita, Osaka 565-0871, Japan.
Nagai
Takayoshi
T
Hirao
Toshikazu
T
D000409:Alanine / Q000737:chemistry*; D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D004151:Dipeptides / Q000737:chemistry*; D005296:Ferrous Compounds / Q000737:chemistry*; D006860:Hydrogen Bonding; D000075163:Metallocenes; D008958:Models, Molecular; D015394:Molecular Structure; D011392:Proline / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013237:Stereoisomerism
D004151:Dipeptides; D005296:Ferrous Compounds; D000075163:Metallocenes; D011392:Proline; D000409:Alanine; C004998:ferrocene