441353-47-5Relevant academic research and scientific papers
Incorporation of Ahc into model dipeptides as an inducer of a β-turn with a distorted amide bond. Conformational analysis
Avenoza, Alberto,Busto, Jesus H.,Peregrina, Jesus M.,Rodriguez, Fernando
, p. 4241 - 4249 (2007/10/03)
The proline residue of dipeptides Ser-Pro and Pro-Ser has been replaced by 7-azabicyclo[2.2.1]heptane-1-carboxylic acid (Ahc), a conformationally restricted analogue of proline that is capable of mimicking distorted amides.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.
Effect of sequence on peptide geometry in 5-tert-butylprolyl type VI β-turn mimics
Halab, Liliane,Lubell, William D.
, p. 2474 - 2484 (2007/10/03)
The influence of sequence on turn geometry was examined by incorporating (2S,5R)-5-tert-butylproline (5-tBuPro) into a series of dipeptides and tetrapeptides. (2S,5R)-5-tert-Butylproline and proline were respectively introduced at the C-termina
