2024-03-28T19:20:08Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/1560992020-05-11T09:58:53Zcom_10261_52707com_10261_5com_10261_31com_10261_3col_10261_52715col_10261_410
2017-10-05T11:36:19Z
urn:hdl:10261/156099
Urdine amino acids conjugates as buiding blocks for bisubstrate inhibitors
Ghirardello, Mattia
Delso, J. Ignacio
Tejero, Tomás
Merino, Pedro
Resumen 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.
During 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.
2017-10-05T11:36:19Z
2017-10-05T11:36:19Z
2016
póster de congreso
XIII Simposio de Investigadores Jóvenes RSEQ Sigma-Aldrich (2016)
http://hdl.handle.net/10261/156099
eng
Sí
closedAccess