Effect of beta-O-glucosylation on L-Ser and L-Thr Diamides: A Bias toward alfa-Helical Conformations
- Corzana, F. 2
- Busto, J.H. 2
- Engelsen, S.B. 4
- Jiménez-Barberó, J. 1
- Asensio, J.L. 3
- Peregrina, J.M. 2
- Avenoza, A. 2
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1
Centro de Investigaciones Biológicas
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2
Universidad de La Rioja
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3
Instituto de Química Orgánica General
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4
University of Copenhagen
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ISSN: 0947-6539
Año de publicación: 2006
Volumen: 12
Número: 30
Páginas: 7864-7871
Tipo: Artículo
beta Ver similares en nube de resultadosOtras publicaciones en: Chemistry - A European Journal
Resumen
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,.