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Towards new glycosyltransferase ligands

AuthorsGhirardello, Mattia ; Delso, J. Ignacio; Tejero, Tomás ; Martín-Santamaría, Sonsoles ; Hurtado-Guerrero, Ramón; Merino, Pedro
Issue Date2015
CitationXII Simposio de Investigadores Jóvenes RSEQ Sigma-Aldrich (2015)
AbstractGalNAc‐T2 is an enzyme that catalyze the transfer of N-­Acetylgalactosamine from the donor substrate UDP‐GalNAc to the acceptor hydroxyl groups in mucine-‐type proteins. It belongs to a wide family of glycosyltransferase of which twenty isoforms are present in the human body. At the present time, despite the importance of this enzyme, involved in several metabolic disorders; very few binding substrates exists for this family of enzymes and no inhibitors have been reported. Here, we propose a new method to generate a new family of α-C‐glycoside ligands, based on the reactivity of the phosphonate group, miming the natural substrate but suppressing one phosphate function; leading to a new class of non‐too polar and non-­hydrolyzable compounds. We standardize the synthesis on a wide pool of different carbohydrates. Afterwards a docking study confirmed the binding capability of these new molecules with the GalNAc-­T2 enzyme and a biological assay and a crystal structure validated the in-­silico predicted binding capability. This method can be efficiently used to synthetize a wide variety of new compounds, and is easily extendable to different class of molecules and nucleosides to find new glycosyltransferase ligands.
DescriptionResumen del trabajo presentado al XII Simposio de Investigadores Jóvenes de la Real Sociedad Española de Química Sigma-Aldrich, celebrado en Barcelona del 3 al 6 de noviembre de 2015.
Appears in Collections:(ISQCH) Comunicaciones congresos
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