English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/156099
logo share SHARE   Add this article to your Mendeley library MendeleyBASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:


Urdine amino acids conjugates as buiding blocks for bisubstrate inhibitors

AuthorsGhirardello, Mattia ; Delso, J. Ignacio; Tejero, Tomás ; Merino, Pedro
Issue Date2016
CitationXIII Simposio de Investigadores Jóvenes RSEQ Sigma-Aldrich (2016)
AbstractDuring the last years bisubstrate inhibitors are playing a growing role in drug design, finding an intense application in enzymes such as glycosyltransferases. Recently this approach was used to build selective ligands targeting the OGlcNAc transferase (OGT) in which the donor (uridine based), and the acceptor (peptide based) moieties, are covalently linked in a single substrate. However; the synthesis of these ligands usually involves low yield and difficult synthetic pathways. Herein we present an efficient protocol for the synthesis of useful N-Fmoc-protected, uridine-based amino acids; that can be directly employed as building blocks in solid-phase peptide synthesis. Furthermore, these amino acids were functionalized with different linker between the uridine and the amino acidic fragment giving the possibility to play with neutral or coordinating uridine-peptide bridges, making of them a versatile synthetic instrument to build new inhibitors targeting OGT and more uridinebased glycosyltransferases.
DescriptionResumen del póster presentado al XIII Simposio de Investigadores Jóvenes de la Real Sociedad Española de Química Sigma-Aldrich, celebrado en Logroño del 8 al 11 de noviembre de 2016.
Appears in Collections:(ISQCH) Comunicaciones congresos
(ICMA) Comunicaciones congresos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
Show full item record
Review this work

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