Conformational analysis of peptides and glycopeptides derived from the consensus sequence for β-O-glucosylation

  1. Somovilla, V.J. 2
  2. Martínez-Sáez, N. 2
  3. Fernández-Tejada, A. 1
  4. García De La Torre, Beatriz 5
  5. Andreu, D. 5
  6. Jiménez-Barbero, J. 136
  7. Asensio, J.L. 4
  8. Avenoza, A. 2
  9. Busto, J.H. 2
  10. Corzana, F. 2
  11. Peregrina, J.M. 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 IKERBASQUE, Basque Foundation for Science, Bilbao, Spain
  4. 4 Instituto de Química Orgánica General
    info

    Instituto de Química Orgánica General

    Madrid, España

    ROR https://ror.org/05e0q7s59

  5. 5 Universitat Pompeu Fabra
    info

    Universitat Pompeu Fabra

    Barcelona, España

    ROR https://ror.org/04n0g0b29

  6. 6 Structural Biology Unit, CIC bioGUNE, Parque Tecnologico de Bizkaia Building 801A, Derio, Spain
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Journal:
Current Topics in Medicinal Chemistry

ISSN: 1568-0266

Year of publication: 2014

Volume: 14

Issue: 23

Pages: 2712-2721

Type: Article

SCOPUS: 2-s2.0-84926315516 WoS: WOS:000347454500009 GOOGLE SCHOLAR

More publications in: Current Topics in Medicinal Chemistry

Abstract

Cys-Xxx-Ser-Xxx-Pro-Cys (Xxx= any amino acid but Pro) is the most common sequence present in naturally occurring peptides and proteins glycosylated with β-O-glucose (β-O-Glc). Taking into account the lack of studies concerning the spatial disposition of this sequence, we have synthesized and analyzed, in aqueous solution, the conformational behavior of peptides and a glycopeptide derived from the particular fragment Cys-Ala-Ser-Ser-Pro-Cys. This sequence is found in the crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor. Our studies, based on the use of NOESY experiments in combination with molecular dynamics (MD) simulations, indicate that for this particular fragment, initially characterized by a type I β-turn motif, the glycosylation with β-O-Glc forces the peptide backbone into an extended conformation. This conformation is stabilized by the presence of both hydrogen bonds and water pockets between the peptide and the sugar moieties. © 2014 Bentham Science Publishers.