English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/156178
logo share SHARE   Add this article to your Mendeley library MendeleyBASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Exportar a otros formatos:

DC FieldValueLanguage
dc.contributor.authorGhirardello, Mattiaes_ES
dc.contributor.authorDelso, J. Ignacioes_ES
dc.contributor.authorTejero, Tomáses_ES
dc.contributor.authorMartín-Santamaría, Sonsoleses_ES
dc.contributor.authorHurtado-Guerrero, Ramónes_ES
dc.contributor.authorMerino, Pedroes_ES
dc.identifier.citationBIFI 2016es_ES
dc.descriptionResumen del póster presentado a la VII International Conference on Molecular Recognition, celebrada en Zaragoza (España) del 1 al 3 de febrero de 2016.es_ES
dc.description.abstractGalNAc-T2, is an enzyme belonging to the glycosyltransferase family that catalyzes the transfer of N-Acetylgalactosamine, from the donor substrate UDP-GalNAc to the acceptor hydroxyl groups in mucine-type proteins. This constitutes the most complex and well-regulated type of protein O-glycosylation, which present twenty different isoforms in the human body. Despite the important role that the protein plays, from health to metabolic disorders and disease, at the present time very few ligands have been reported, of which none is an effective inhibitor. In this work we propose a synthetic method directing to a new class of glycomimetic ligands, capable to bind the protein in the active site. These ligands leading to non-hydrolisable and less polar uridine-phosphonate derivatives, in which one phosphate function was suppressed and substitute by an alkyl chain, are by far more stable than the natural substrate. The synthetic method has been standardized on a wide pool of different carbohydrates; afterwards the protein binding capability was confirmed by a docking study and biological test too. Finally, a crystal structure of the complex [GalNAc-T2 – ligand] confirms the predicted binding capability, validating this method as a powerful and versatile tool in order to synthetize new glycosyltransferase inhibitors.es_ES
dc.titleNew glycomimetics targeting human GalNAc-T2, synthesis, computational and structural studieses_ES
dc.typepóster de congresoes_ES
dc.description.peerreviewedPeer reviewedes_ES
oprm.item.hasRevisionno ko 0 false*
Appears in Collections:(ISQCH) Comunicaciones congresos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
Show simple item record

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.