Dynamics and Hydration Properties of Small Antifreeze-Like Glycopeptides Containing Non- natural Amino Acids
- Corzana, F. 1
- Busto, J.H. 1
- De Luis, M.G. 1
- Fernández-Tejada, A. 1
- Rodríguez, F. 1
- Jiménez-Barbero, J. 2
- Avenoza, A. 1
- Peregrina, J.M. 1
-
1
Universidad de La Rioja
info
-
2
Centro de Investigaciones Biológicas
info
ISSN: 1434-193X
Year of publication: 2010
Volume: 18
Pages: 3525-3532
Type: Article
More publications in: European Journal of Organic Chemistry
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.