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Título: | Detection and Quantitative Analysis of Two Independent Binding Modes of a Small Ligand Responsible for DC-SIGN Clustering |
Autor: | Guzzi, Cinzia CSIC ORCID; Alfarano, Pietro; Sutkeviciute, Ieva; Sattin, Sara; Ribeiro-Viana, Renato CSIC ORCID; Fieschi, Franck; Bernardi, Anna; Weiser, Joerg; Rojo, Francisco Javier ; Angulo, Jesús CSIC ORCID ; Nieto, Pedro M. CSIC ORCID | Fecha de publicación: | 2015 | Editor: | Royal Society of Chemistry (UK) | Citación: | Organic and Biomolecular Chemistry, 14: 335-344(2015) | Resumen: | DC-SIGN (dendritic cell-specific ICAM-3 grabbing non-integrin) is a C-type lectin receptor (CLR) present, mainly in dendritic cells (DCs), as one of the major pattern recognition receptors (PRRs). This receptor has a relevant role in viral infection processes. Recent approaches aiming to block DC-SIGN have been presented as attractive anti-HIV strategies. DC-SIGN binds mannose or fucose-containing carbohydrates from viral proteins such as the HIV envelope glycoprotein gp120. We have previously demonstrated that multivalent dendrons bearing multiple copies of glycomimetic ligands were able to inhibit DC-SIGN-dependent HIV infection in cervical explant models. Optimization of glycomimetic ligands requires detailed characterization and analysis of their binding modes because they notably influence binding affinities. In a previous study we characterized the binding mode of DC-SIGN with ligand 1, which shows a single binding mode as demonstrated by NMR and X-ray crystallography. In this work we report the binding studies of DC-SIGN with pseudotrisaccharide 2, which has a larger affinity. Their binding was analysed by TR-NOESY and STD NMR experiments, combined with the CORCEMA-ST protocol and molecular modelling. These studies demonstrate that in solution the complex cannot be explained by a single binding mode. We describe the ensemble of ligand bound modes that best fit the experimental data and explain the higher inhibition values found for ligand 2. | Versión del editor: | http://dx.doi.org/10.1039/C5OB02025E | URI: | http://hdl.handle.net/10261/127818 | DOI: | 10.1039/C5OB02025E |
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