Effect of beta-O-glucosylation on L-Ser and L-Thr Diamides: A Bias toward alfa-Helical Conformations

  1. Corzana, F. 2
  2. Busto, J.H. 2
  3. Engelsen, S.B. 4
  4. Jiménez-Barberó, J. 1
  5. Asensio, J.L. 3
  6. Peregrina, J.M. 2
  7. Avenoza, A. 2
  1. 1 Centro de Investigaciones Biológicas
    info

    Centro de Investigaciones Biológicas

    Madrid, España

    ROR https://ror.org/04advdf21

  2. 2 Universidad de La Rioja
    info

    Universidad de La Rioja

    Logroño, España

    ROR https://ror.org/0553yr311

  3. 3 Instituto de Química Orgánica General
    info

    Instituto de Química Orgánica General

    Madrid, España

    ROR https://ror.org/05e0q7s59

  4. 4 University of Copenhagen
    info

    University of Copenhagen

    Copenhague, Dinamarca

    ROR https://ror.org/035b05819

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Journal:
Chemistry - A European Journal

ISSN: 0947-6539

Year of publication: 2006

Volume: 12

Issue: 30

Pages: 7864-7871

Type: Article

beta Ver similares en nube de resultados
DOI: 10.1002/CHEM.200600128 PMID: 16850514 SCOPUS: 2-s2.0-33750374695 WoS: WOS:000241469300012 GOOGLE SCHOLAR

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Abstract

β-D-O-glucosylation produces a remarkable effect on the peptide backbone of the model peptides derived from serine and threonine. Consequently, this type of glycosylation is responsible for the experimentally observed shift from extended conformations (model peptides) towards the folded conformations (model glycopeptides). The conclusion has been solidly assessed by a combined NMR/MD protocol. Interestingly, the MD (molecular dynamics) results for the glycopeptides point towards the existence of waterbridging molecules between the sugar and peptide moieties, which could explain the stabilization of the folded conformers in aqueous solution. © 2006 Wiley-VCH Verlag GmbH & Co, KGaA,.