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Unique DC-SIGN clustering activity of a small glycomimetic: a lesson for ligand design

Opened Access Unique DC-SIGN clustering activity of a small glycomimetic: a lesson for ligand design

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Autor: Sutkeviciute, Ieva
Thépaut, Michel
Sattin, Sara
Berzi, Angela
McGeagh, John
Grudinin, Sergei
Weiser, Jöerg
Le Roy, Aline
Reina, José J.
Rojo, Javier
Clerici, Mario
Bernardi, Anna
Fecha: 2014
Publicado en: ACS Chemical Biology, 9 (6), 1377-1385.
Tipo de documento: Artículo
Resumen: DC-SIGN is a dendritic cell-specific C-type lectin receptor that recognizes highly glycosylated ligands expressed on the surface of various pathogens. This receptor plays an important role in the early stages of many viral infections, including HIV, which makes it an interesting therapeutic target. Glycomimetic compounds are good drug candidates for DC-SIGN inhibition due to their high solubility, resistance to glycosidases, and nontoxicity. We studied the structural properties of the interaction of the tetrameric DC-SIGN extracellular domain (ECD), with two glycomimetic antagonists, a pseudomannobioside (1) and a linear pseudomannotrioside (2). Though the inhibitory potency of 2, as measured by SPR competition experiments, was 1 order of magnitude higher than that of 1, crystal structures of the complexes within the DC-SIGN carbohydrate recognition domain showed the same binding mode for both compounds. Moreover, when conjugated to multivalent scaffolds, the inhibitory potencies of t...
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Cita: Sutkeviciute, I., Thépaut, M., Sattin, S., Berzi, A., McGeagh, J., Grudinin, S.,...,Bernardi, A. (2014). Unique DC-SIGN clustering activity of a small glycomimetic: a lesson for ligand design. ACS Chemical Biology, 9 (6), 1377-1385.
Tamaño: 1.113Mb
Formato: PDF

URI: https://hdl.handle.net/11441/69681

DOI: 10.1021/cb500054h

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