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The Nature and Sequence of the Amino Acid Aglycone Strongly Modulates the Conformation and Dynamics Effects of Tn Antigen´s Clusters

AutorCorzana, Francisco; Busto, Jesús H.; García de Luis, Marisa; Jiménez-Barbero, Jesús ; Avenoza, Alberto; Peregrina, J.M.
Palabras claveAntigens
conformation analysis
molecular dynamics
NMR spectroscopy
Fecha de publicación6-abr-2009
CitaciónChemistry - A European Journal, 15 (15) : 3863-3874 (2009)
ResumenSynthetic oligosaccharide vaccines based on carbohydrate epitopes are currently being evaluated as potential immunotherapeutics in the treatment of cancer. In an effort to study the role that the amino acid moiety (l-serine and/or l-threonine residues) plays on the global shape of the resulting glycopeptides and on the dynamics of the carbohydrate moiety, diverse glycopeptides based on the Tn antigen have been synthesized and studied in aqueous solution by combin- ing NMR spectroscopic experiments and molecular dynamics simulations. Our results demonstrate that although the effect of the clustering of Tn on the peptide backbone is not remarkable, it substantially modifies the dynamics, and thus, the presentation features of the carbohydrate moiety. In fact, the selected sequence has a crucial influ- ence on both the orientation and flexi- bility of the sugar region. Thus, al- though a serine–threonine pair shows a well-defined spatial disposition of the Tn epitopes, its analogue sequence threonine–serine allows a certain degree of mobility that could favor the interaction with a diversity of receptors without a major energy penalty. These features can be explained by attending to the different conformational behav- ior of the glycosidic linkage of threo- nine-containing glycopeptides when compared with those of the serine ana- logues. On this basis, and taking into account that these carbohydrates inter- act with components of the immune system, these findings could have im- plications for further design of new cancer vaccines
Descripción12 páginas, 10 figuras, 2 tablas -- PAGS nros. 3863-3874
Versión del editorhttp://dx.doi.org/10.1002/chem.200801777
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