Incorporation of Ahc into Model Dipeptides as an Inducer of a
β-Turn with a Distorted Amide Bond. Conformational Analysis

Avenoza, Alberto; Busto, Jesús H.; Peregrina, Jesús M.; Rodríguez, Fernando

doi:10.1021/jo016406r.s001

jo016406r_si_001.pdf (3.31 MB)

Incorporation of Ahc into Model Dipeptides as an Inducer of a β-Turn with a Distorted Amide Bond. Conformational Analysis

journal contribution

posted on 2002-05-17, 00:00 authored by Alberto Avenoza, Jesús H. Busto, Jesús M. Peregrina, Fernando Rodríguez

The proline residue of dipeptides Ser-Pro and Pro-Ser has been replaced by 7-azabicyclo[2.2.1]heptane-1-carboxylic acid (Ahc), a conformationally restricted analogue of proline that is capable of mimicking distorted amides.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.