dc.contributor.author | Martínez, José Daniel | |
dc.contributor.author | Valverde, Pablo | |
dc.contributor.author | Delgado, Sandra | |
dc.contributor.author | Romanó, Cecilia | |
dc.contributor.author | Linclau, Bruno | |
dc.contributor.author | Reichardt, Niels Christian | |
dc.contributor.author | Oscarson, Stefan | |
dc.contributor.author | Ardá, Ana | |
dc.contributor.author | Jiménez Barbero, Jesús | |
dc.contributor.author | Cañada Vicinay, Francisco Javier | |
dc.date.accessioned | 2020-02-12T10:06:21Z | |
dc.date.available | 2020-02-12T10:06:21Z | |
dc.date.issued | 2019-06-25 | |
dc.identifier.citation | Molecules 24(12) : (2019) // Article ID 2337 | es_ES |
dc.identifier.issn | 1420-3049 | |
dc.identifier.uri | http://hdl.handle.net/10810/40566 | |
dc.description.abstract | A fluorine nuclear magnetic resonance (F-19-NMR)-based method is employed to assess the binding preferences and interaction details of a library of synthetic fluorinated monosaccharides towards dendritic cell-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN), a lectin of biomedical interest, which is involved in different viral infections, including HIV and Ebola, and is able to recognize a variety of self- and non-self-glycans. The strategy employed allows not only screening of a mixture of compounds, but also obtaining valuable information on the specific sugar-protein interactions. The analysis of the data demonstrates that monosaccharides Fuc, Man, Glc, and Gal are able to bind DC-SIGN, although with decreasing affinity. Moreover, a new binding mode between Man moieties and DC-SIGN, which might have biological implications, is also detected for the first time. The combination of the F-19 with standard proton saturation transfer difference (H-1-STD-NMR) data, assisted by molecular dynamics (MD) simulations, permits us to successfully define this new binding epitope, where Man coordinates a Ca2+ ion of the lectin carbohydrate recognition domain (CRD) through the axial OH-2 and equatorial OH-3 groups, thus mimicking the Fuc/DC-SIGN binding architecture. | es_ES |
dc.description.sponsorship | We thank Agencia Estatal de Investigacion (Spain) for grants CTQ2015-64597-C2-1-P and 2-P, CTQ2015-68756-R, and for FPI and FPU fellowships to J.D.M. and P.V., respectively, and for the Severo Ochoa Excellence Accreditation (SEV-2016-0644). J.J.-B. also thanks the European Research Council (RECGLYCANMR, Advanced Grant no. 788143). | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | MDPI | es_ES |
dc.relation | info:eu-repo/grantAgreement/EC/H2020/788143 | es_ES |
dc.rights | info:eu-repo/semantics/openAccess | es_ES |
dc.rights.uri | http://creativecommons.org/licenses/by/3.0/es/ | * |
dc.subject | NMR | es_ES |
dc.subject | molecular recognition | es_ES |
dc.subject | lectin | es_ES |
dc.subject | glycomimetics | es_ES |
dc.subject | DC-SIGN | es_ES |
dc.subject | C-type lectins | es_ES |
dc.subject | fluorinated sugars | es_ES |
dc.subject | F-19-NMR | es_ES |
dc.subject | screening | es_ES |
dc.subject | molecular dynamics | es_ES |
dc.subject | transfer difference NMR | es_ES |
dc.subject | structural basis | es_ES |
dc.subject | recognition | es_ES |
dc.subject | protein | es_ES |
dc.subject | ligand | es_ES |
dc.subject | parameters | es_ES |
dc.subject | langerin | es_ES |
dc.subject | glycans | es_ES |
dc.title | Unraveling Sugar Binding Modes to DC-SIGN by Employing Fluorinated Carbohydrates | es_ES |
dc.type | info:eu-repo/semantics/article | es_ES |
dc.rights.holder | This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0) | es_ES |
dc.rights.holder | Atribución 3.0 España | * |
dc.relation.publisherversion | https://www.mdpi.com/1420-3049/24/12/2337 | es_ES |
dc.identifier.doi | 10.3390/molecules24122337 | |
dc.contributor.funder | European Commission | |
dc.departamentoes | Química orgánica II | es_ES |
dc.departamentoeu | Kimika organikoa II | es_ES |