Exploring carbohydrate-peptide interactions in the gas phase: Structure and selectivity in complexes of pyranosides with N-acetylphenylalanine methylamide

Emilio J. Cocinero, Pierre Çarçabal, Timothy D. Vaden, Benjamin G. Davis, John P. Simons

Research output: Contribution to journalArticlepeer-review

28 Scopus citations

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 β 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.

Original languageEnglish (US)
Pages (from-to)4548-4557
Number of pages10
JournalJournal of the American Chemical Society
Volume133
Issue number12
DOIs
StatePublished - Mar 30 2011

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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