Engineering O-glycosylation Points in Non-extended Peptides: Implications for the Molecular Recognition of Short Tumor-associated Glycopeptides

  1. Corzana, F. 3
  2. Busto, J.H. 3
  3. Marcelo, F. 1
  4. Garcíadeluis, M. 3
  5. Asensio, J.L. 4
  6. Martín-Santamaría, S. 2
  7. Jiménez-Barbero, J. 1
  8. Avenoza, A. 3
  9. Peregrina, J.M. 3
  1. 1 Centro de Investigaciones Biológicas
    info

    Centro de Investigaciones Biológicas

    Madrid, España

    ROR https://ror.org/04advdf21

  2. 2 Universidad CEU San Pablo
    info

    Universidad CEU San Pablo

    Madrid, España

    ROR https://ror.org/00tvate34

  3. 3 Universidad de La Rioja
    info

    Universidad de La Rioja

    Logroño, España

    ROR https://ror.org/0553yr311

  4. 4 Instituto de Química Orgánica General
    info

    Instituto de Química Orgánica General

    Madrid, España

    ROR https://ror.org/05e0q7s59

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Journal:
Chemistry - A European Journal

ISSN: 0947-6539

Year of publication: 2011

Volume: 17

Issue: 11

Pages: 3105-3110

Type: Article

DOI: 10.1002/CHEM.201003124 SCOPUS: 2-s2.0-79952126046 WoS: WOS:000288098800011 GOOGLE SCHOLAR

More publications in: Chemistry - A European Journal

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Abstract

The ties that bind: The incorporation of non-natural residues in the peptide backbone allows the design of O-glycosylation points in helical segments. This strategy could help to modulate the binding properties between glycopeptides and their protein receptors, such as lectins and antibodies. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.