Structural insight into the aggregation of L-prolyl dipeptides and its effect on organocatalytic performance.
Org Biomol Chem
; 13(2): 592-600, 2015 Jan 14.
Article
em En
| MEDLINE
| ID: mdl-25382228
ABSTRACT
NMR and organocatalytic studies of four dipeptides derived from L-proline are described. Results indicate that important conformational changes around the catalytic L-proline moiety are observed for free dipeptides upon changing the adjacent amino acid. Also, an aggregation process is detected as the concentration increases. The self-association of the dipeptides has been fitted to a cooperative binding model. All the compounds have been assayed as catalysts for the conjugated addition of cyclohexanone to trans-ß-nitrostyrene in toluene. In agreement with the structural studies, noticeable changes in the catalytic performance are detected upon changing the catalyst concentration, as the catalyst is activated by self-aggregation.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Compostos Orgânicos
/
Prolina
/
Dipeptídeos
Idioma:
En
Revista:
Org Biomol Chem
Assunto da revista:
BIOQUIMICA
/
QUIMICA
Ano de publicação:
2015
Tipo de documento:
Article