Incorporation of Ahc into Model Dipeptides as an Inducer of a Beta-Turn with a Distorted Amide Bond. Conformational Analysis
- Avenoza, A. 1
- Busto, J.H. 1
- Peregrina, J.M. 1
- Rodríguez, F. 1
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1
Universidad de La Rioja
info
ISSN: 0022-3263
Año de publicación: 2002
Volumen: 67
Número: 12
Páginas: 4241-4249
Tipo: Artículo
beta Ver similares en nube de resultadosOtras publicaciones en: Journal of Organic Chemistry
Resumen
The proline residue of dipeptides Ser-Pro and Pro-Ser has been replaced by 7-azabicyclo[2.2.1]heptane-1-carboxylic acid (Ahc), a conformationally restricted analogue of proline that is capable of mimicking distorted amides. The conformational analysis of the new peptides in the solid state revealed that the Ahc-Ser sequence displays a type I β-turn, which includes a distorted amide bond. In contrast, the Ser-Ahc sequence exists in a nonfolded structure.