Highly ordered structures of peptides by using molecular scaffolds.
Protein secondary structures such as alpha-helices, beta-sheets, and beta-turns are important in inducing the three-dimensional structure and biological activity of proteins. Designing secondary structure mimics composed of short peptides has attracted much attention not only to gain fundamental insight into the factors affecting protein folding but also to develop pharmacologically useful compounds, artificial receptors, asymmetric catalysts, and new materials. In this tutorial review, we focus on molecular scaffolds employed to induce beta-sheet-like structure in attached peptide chains, thereby creating highly ordered molecular structures, and discuss the versatility of these molecular scaffolds to regulate the attached peptide strands in the appropriate dimensions.
Department of Applied Chemistry, Graduate School of Engineering, Osaka University, Yamada-oka, Suita, Osaka 565-0871, Japan.
Toshiyuki
T
Moriuchi
Toshikazu
T
Hirao
D005296:Ferrous Compounds / Q000737:chemistry; D006860:Hydrogen Bonding; D000075163:Metallocenes; D008958:Models, Molecular; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry*; D010456:Peptides, Cyclic / Q000138:chemical synthesis* / Q000737:chemistry; D017510:Protein Folding; D017433:Protein Structure, Secondary
D005296:Ferrous Compounds; D000075163:Metallocenes; D010455:Peptides; D010456:Peptides, Cyclic; C004998:ferrocene