NMR and molecular recognition: The interaction of human galectin-8 and DC-SIGN with natural glycans and glycomimetics.
Glycans are everywhere in Nature, where they play a plethora of functions in every domain of life. The recognition of glycans by lectins is at the heart of a myriad of biological proceses, including host-pathogen interactions, which have made them essential targets in the field of drug discovery. In...
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| Tipo de recurso: | tesis doctoral |
| Fecha de publicación: | 2023 |
| País: | España |
| Institución: | Universidad del País Vasco |
| Repositorio: | Addi. Archivo Digital para la Docencia y la Investigación |
| OAI Identifier: | oai:addi.ehu.eus:10810/60824 |
| Acceso en línea: | http://hdl.handle.net/10810/60824 |
| Access Level: | acceso embargado |
| Palabra clave: | magnetic resonance spectroscopy glucides proteins espectroscopia de resonancia magnética glúcidos proteínas |
| Sumario: | Glycans are everywhere in Nature, where they play a plethora of functions in every domain of life. The recognition of glycans by lectins is at the heart of a myriad of biological proceses, including host-pathogen interactions, which have made them essential targets in the field of drug discovery. In this context, the main focus of this Thesis has centred on unravelling of the conformational and structural properties of the recognition of a battery of natural and synthetically obtained glycans to two specific human lectins, galectin-8 and DC-SIGN. This analysis has been performed employing a synergic combination of NMR-based methods, assisted by other experimental methods (ITC) and computational tools (Molecular Dynamics simulations). |
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