Exploring carbohydrate-peptide interactions in the gas phase: structure and selectivity in complexes of pyranosides with N-acetylphenylalanine methylamide.
J Am Chem Soc
; 133(12): 4548-57, 2011 Mar 30.
Article
em En
| MEDLINE
| ID: mdl-21375248
ABSTRACT
The physical basis of carbohydrate-peptide interactions has been explored by probing the structures of a series of complexes generated in a solvent-free environment under molecular beam conditions. A combination of double-resonance IR-UV spectroscopy and quantum-chemical calculations has established the structures of complexes of the model, N-acetyl-L-phenylalanine methylamide, bound to the α and ß anomers of methyl D-gluco- and D-galactopyranoside as guests. In all cases, the carbohydrates are bound through hydrogen bonding to the dipeptide chain, although with some differing patterns. The amino acid host "engages" with the most suitable pair of neighboring conjugate sites on each carbohydrate; the specific choice depends on the conformation of the peptide backbone and the configuration and conformation of the carbohydrate ligand. None of the structures is supported by "stacking" interactions with the aromatic ring, despite their common occurrence in bound carbohydrate-protein structures.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fenilalanina
/
Galactose
Idioma:
En
Revista:
J Am Chem Soc
Ano de publicação:
2011
Tipo de documento:
Article