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Urdine amino acids conjugates as buiding blocks for bisubstrate inhibitors

AutorGhirardello, Mattia ; Delso, J. Ignacio; Tejero, Tomás ; Merino, Pedro
Fecha de publicación2016
CitaciónXIII Simposio de Investigadores Jóvenes RSEQ Sigma-Aldrich (2016)
ResumenDuring 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.
DescripciónResumen 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.
URIhttp://hdl.handle.net/10261/156099
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