Dynamics and Hydration Properties of Small Antifreeze-Like Glycopeptides Containing Non- natural Amino Acids

  1. Corzana, F. 1
  2. Busto, J.H. 1
  3. De Luis, M.G. 1
  4. Fernández-Tejada, A. 1
  5. Rodríguez, F. 1
  6. Jiménez-Barbero, J. 2
  7. Avenoza, A. 1
  8. Peregrina, J.M. 1
  1. 1 Universidad de La Rioja
    info

    Universidad de La Rioja

    Logroño, España

    GRID grid.119021.a

  2. 2 Centro de Investigaciones Biológicas
    info

    Centro de Investigaciones Biológicas

    Madrid, España

    GRID grid.418281.6

Journal:
European Journal of Organic Chemistry

ISSN: 1434-193X

Year of publication: 2010

Volume: 18

Pages: 3525-3532

Type: Article

Export: RIS
DOI: 10.1002/ejoc.201000375 SCOPUS: 2-s2.0-77953284506 WoS: 000279746300020 GOOGLE SCHOLAR

Metrics

Cited by

  • Scopus Cited by: 11 (12-06-2021)

Journal Citation Reports

  • Year 2010
  • Journal Impact Factor: 3.206
  • Best Quartile: Q1
  • Area: CHEMISTRY, ORGANIC Quartile: Q1 Rank in area: 13/56 (Ranking edition: SCIE)

SCImago Journal Rank

  • Year 2010
  • SJR Journal Impact: 1.615
  • Best Quartile: Q1
  • Area: Organic Chemistry Quartile: Q1 Rank in area: 27/174
  • Area: Physical and Theoretical Chemistry Quartile: Q1 Rank in area: 26/161

Abstract

Novel studies on the synthesis and conformation in aqueous solution of three antifreeze-like glycopeptides containing the sequence Xaa(α-GalNAc)- Ala-Ala, with Xaa being threonine (Thr) or the non-natural amino acids α-methylserine (MeSer) or α-methylthreonine (MeThr), are reported. The study has combined NMR experiments with molecular dynamics simulations. Whereas the Thr derivative is rather rigid in solution and exhibits an extended conformation for the backbone, the non-natural glycopeptides are fairly flexible and show random coil structures for the peptide sequence. On the other hand, only those glycopeptides with a methyl group at Cβ of the underlying amino acid show perpendicular orientation of the sugar with respect to the peptide moiety. This structural feature, together with the rigidity of the Thr-containing glycopeptide, makes this system unique to structure the water molecules of its first hydration shell. In addition, despite its chemical similarity, the different observed conformational behaviors of all these molecules, as well as the differences in their dynamics and hydration properties, make them suitable systems to shed light on the key factors that govern antifreeze activity. © 2010 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.