2024-03-29T06:52:07Zhttps://repositori.uji.es/oai/requestoai:repositori.uji.es:10234/1593712023-09-26T12:49:50Zcom_10234_7053com_10234_9col_10234_8639
00925njm 22002777a 4500
dc
Berdugo Gumbau, Cristina
author
Escuder, Beatriu
author
Miravet, Juan
author
2015
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-
β-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.
Org. Biomol. Chem., 2015, 13, 592
1477-0539
1477-0520
http://hdl.handle.net/10234/159371
http://dx.doi.org/10.1039/C4OB02003K
1,4-addition reactions
methanolytic desymmetrization
bifunctional organocatalyst
asymmetric catalysis
conjugate addition
cyclic anhydrides
enamine catalysis
beta-nitrostyrene
aldol reactions
nitro olefins
Structural insight into the aggregation of L-prolyl dipeptides and its effect on organocatalytic performance