Structural insight into the aggregation of L-prolyl dipeptides and its effect on organocatalytic performance
comunitat-uji-handle:10234/9
comunitat-uji-handle2:10234/7053
comunitat-uji-handle3:10234/8639
comunitat-uji-handle4:
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http://dx.doi.org/10.1039/C4OB02003K |
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Title
Structural insight into the aggregation of L-prolyl dipeptides and its effect on organocatalytic performanceDate
2015Publisher
Royal Society of ChemistryISSN
1477-0539; 1477-0520Bibliographic citation
Org. Biomol. Chem., 2015, 13, 592Type
info:eu-repo/semantics/articleSubject
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 ... [+]
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. [-]
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Org. Biomol. Chem., 2015, 13, 592–600Rights
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This journal is © The Royal Society of Chemistry 2015
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