4.8 Article

Exploring Carbohydrate-Peptide Interactions in the Gas Phase: Structure and Selectivity in Complexes of Pyranosides with N-Acetylphenylalanine Methylamide

Journal

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 133, Issue 12, Pages 4548-4557

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/ja109664k

Keywords

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Funding

  1. Leverhulme Trust
  2. Royal Society
  3. Wolfson Foundation
  4. EPSRC
  5. Spanish Ministry (MICINN)
  6. Royal Society, USA/Canada
  7. Linacre College
  8. BBSRC [BB/E004350/1] Funding Source: UKRI
  9. EPSRC [EP/E000614/1, EP/I500200/1, EP/G026688/1, EP/G03088X/1] Funding Source: UKRI
  10. Biotechnology and Biological Sciences Research Council [BB/C510824/1, BB/E004350/1, EGA17763] Funding Source: researchfish
  11. Engineering and Physical Sciences Research Council [EP/E000614/1, EP/D023335/1, GR/T26542/01, EP/G03088X/1, EP/G026688/1, EP/I500200/1, EP/D023343/1] Funding Source: researchfish

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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 alpha and beta 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.

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