Andrés González Santana, Laura Díaz-Casado, Laura Montalvillo, Ester Jiménez-Moreno, Enrique Mann and Juan Luis Asensio* Pages 1208 - 1218 ( 11 )
Aromatic platforms are ubiquitous recognition motifs occurring in protein carbohydrate- binding domains (CBDs), RNA receptors and enzymes. They stabilize the glycoside/ receptor complexes by participating in stacking CH/π interactions with either the α- or β- face of the corresponding pyranose units. In addition, the role played by aromatic units in the stabilization of glycoside cationic transition states has started being recognized in recent years. Extensive studies carried out during the last decade have allowed the dissection of the main contributing forces that stabilize the carbohydrate/aromatic complexes, while helping delineate not only the standing relationship between the glycoside/ aromatic chemical structures and the strength of this interaction but also their potential influence on glycoside reactivity.
Carbohydrate recognition, stacking CH/π interactions, cation/π interactions, structure-stability relationships, glycosidic bond formation, carbohydrate-binding domains.
Instituto de Química Orgánica General (IQOG-CSIC), Madrid, Instituto de Química Orgánica General (IQOG-CSIC), Madrid, Instituto de Química Orgánica General (IQOG-CSIC), Madrid, Department of Chemistry, University of La Rioja, Logroño, Instituto de Química Orgánica General (IQOG-CSIC), Madrid, Instituto de Química Orgánica General (IQOG-CSIC), Madrid