| Autor: |
Gatos, M., Formaggio, F., Crisma, M., Valle, G., Toniolo, C., Bonora, G. M., Saviano, M., Menchise, V., Galdiero, S., Pedone, C., Benedetti, E., IACOVINO, Rosa |
| Přispěvatelé: |
Gatos, M., Formaggio, F., Crisma, M., Valle, G., Toniolo, C., Bonora, G. M., Saviano, M., Iacovino, Rosa, Menchise, V., Galdiero, S., Pedone, C., Benedetti, E. |
| Jazyk: |
angličtina |
| Rok vydání: |
1997 |
| Předmět: |
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| Popis: |
A series of N- and C-protected, monodispersed homo-oligopeptides (to the pentamer level) from the cycloaliphatic Cα,α-dialkylated glycine 1-aminocyclononane-1-carboxylic acid (Ac9c) and two Ala/AC9C tripeptides have been synthesized by solution methods and fully characterized. The conformational preferences of all the model peptides were determined in deuterochloroform solution by FT-IR absorption and 1H-NMR. The molecular structures of the amino acid derivatives mClAc-Ac9C-OH and Z-Ac9C-OtBu, the dipeptide pBrBz-(Ac9c)2-OtBu, the tetrapeptide Z-(Ac9c)4-OtBu, and the pentapeptide Z-( Ac9C)5-OtBu were determined in the crystal state by X-ray diffraction. Based on this information, the average geometry and the preferred conformation for the cyclononyl moiety of the Ac9c residue have been assessed. The backbone conformational data are strongly in favour of the conclusion that the Ac9c residue is a strong β-turn and helix former. A comparison with the structural propensity of α-aminoisobutyric acid, the prototype of Cα,α-dialkylated glycines, and the other extensively investigated members of the family of 1-aminocycloalkane-1-carboxylic acids (Acnc, with n=3-8) is made and the implications for the use of the Ac9c residue in conformationally constrained analogues of bioactive peptides are briefly examined. © European Peptide Society and John Wiley & Sons, Ltd. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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