Pseudopeptidic Cages as Receptors for N-Protected Dipeptides
Impacto
Scholar |
Otros documentos de la autoría: Faggi, Enrico; Moure, Alejandra; Bolte, Michael; Vicent Barrera, Cristian; Luis, Santiago V.; Alfonso Rodríguez, Ignacio
Metadatos
Mostrar el registro completo del ítemcomunitat-uji-handle:10234/9
comunitat-uji-handle2:10234/7053
comunitat-uji-handle3:10234/8639
comunitat-uji-handle4:
INVESTIGACIONEste recurso está restringido
http://dx.doi.org/10.1021/jo500629d |
Metadatos
Título
Pseudopeptidic Cages as Receptors for N-Protected DipeptidesAutoría
Fecha de publicación
2014-04Editor
American Chemical SocietyCita bibliográfica
FAGGI, Enrico, et al. Pseudopeptidic Cages as Receptors for N-Protected Dipeptides. The Journal of organic chemistry, 2014, 79.10: 4590-4601.Tipo de documento
info:eu-repo/semantics/articleVersión de la editorial
http://pubs.acs.org/doi/abs/10.1021/jo500629dPalabras clave / Materias
Resumen
The molecular recognition of short peptides is a challenge in supramolecular chemistry, and the use of peptide-like cage receptors represents a promising approach. Here we report the synthesis and characterization of ... [+]
The molecular recognition of short peptides is a challenge in supramolecular chemistry, and the use of peptide-like cage receptors represents a promising approach. Here we report the synthesis and characterization of a diverse family of pseudopeptidic macrobicycles, as well as their binding abilities toward N-protected dipeptides using a combination of different techniques (NMR, ESI-MS, and fluorescence spectroscopy). The cage hosts were assayed for dipeptide binding using competition ESI-MS experiments as high-throughput screening to obtain general trends for the recognition phenomena. Selected hosts were additionally studied by NMR spectroscopy (1H NMR titration and diffusion-ordered spectroscopy experiments) in different solvents. The results unambiguously demonstrated the formation of the [cage·dipeptide] supramolecular complexes and rendered quantitative information about the strength of the interaction (Kass). The structural variables within the pseudopeptidic cage framework that produced a stronger and more selective recognition were thus identified. The cages showed a remarkable selectivity for N-protected dipeptides with an aromatic amino acid at the carboxylic terminus, which prompted us to propose a mode of binding based on polar and nonpolar noncovalent interactions. Accordingly, we faced the molecular recognition of a target dipeptide (Ac-EY-OH) mimicking a biologically relevant sequence by NMR and fluorescence spectroscopy in highly competitive media. [-]
Publicado en
J. Org. Chem., 2014, 79 (10)Derechos de acceso
Copyright © 2014 American Chemical Society
http://rightsstatements.org/vocab/InC/1.0/
info:eu-repo/semantics/restrictedAccess
http://rightsstatements.org/vocab/InC/1.0/
info:eu-repo/semantics/restrictedAccess
Aparece en las colecciones
- QUIO_Articles [689]