New Insights into alfa-GalNAc-Ser Motif: Influence of Hydrogen Bonding versus Solvent Interactions on the Preferred Conformation

  1. Corzana, F. 1
  2. Busto, J.H. 1
  3. Jiménez-Osés, G. 1
  4. Asensio, J.L. 2
  5. Jiménez-Barbero, J. 3
  6. Peregrina, J.M. 1
  7. Avenoza, A. 1
  1. 1 Universidad de La Rioja
    info

    Universidad de La Rioja

    Logroño, España

    ROR https://ror.org/0553yr311

  2. 2 Instituto de Química Orgánica General
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    Instituto de Química Orgánica General

    Madrid, España

    ROR https://ror.org/05e0q7s59

  3. 3 Centro de Investigaciones Biológicas
    info

    Centro de Investigaciones Biológicas

    Madrid, España

    ROR https://ror.org/04advdf21

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Revista:
Journal of the American Chemical Society

ISSN: 0002-7863

Año de publicación: 2006

Volumen: 128

Número: 45

Páginas: 14640-14648

Tipo: Artículo

DOI: 10.1021/JA064539U PMID: 17090050 SCOPUS: 2-s2.0-33750970562 WoS: WOS:000241857200052 GOOGLE SCHOLAR

Otras publicaciones en: Journal of the American Chemical Society

Resumen

The structural features of the mucin-type simplest model, namely, the glycopeptide α-O-GalNAc-L-Ser diamide, have been investigated by combining NMR spectroscopy, molecular dynamics simulations, and DFT calculations. In contrast to previous reports, the study reveals that intramolecular hydrogen bonds between sugar and peptide residues are very weak and, as a consequence, not strong enough to maintain the well-defined conformation of this type of molecule. In fact, the observed conformation of this model glycopeptide can be satisfactorily explained by the presence of water pockets/bridges between the sugar and the peptide moieties. Additionally, DFT calculations reveal that not only the bridging water molecules but also the surrounding water molecules in the first hydration shell are essential to keep the existing conformation. © 2006 American Chemical Society.