Targeting Galectins With Glycomimetics
Among glycan-binding proteins, galectins, beta-galactoside-binding lectins, exhibit relevant biological roles and are implicated in many diseases, such as cancer and inflammation. Their involvement in crucial pathologies makes them interesting targets for drug discovery. In this review, we gather th...
| Autores: | , , , , |
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 2020 |
| País: | España |
| Institución: | Universidad del País Vasco |
| Repositorio: | Addi. Archivo Digital para la Docencia y la Investigación |
| OAI Identifier: | oai:addi.ehu.eus:10810/49824 |
| Acceso en línea: | http://hdl.handle.net/10810/49824 |
| Access Level: | acceso abierto |
| Palabra clave: | :galectins glycomimetics glycans molecular recogntion drug design carbohydrate-recognition domain Thomsen-Friedenreich antigen bovine serum-albumin molecular-dynamics linker length lung fibrosis lectin binding design affinity |
| Sumario: | Among glycan-binding proteins, galectins, beta-galactoside-binding lectins, exhibit relevant biological roles and are implicated in many diseases, such as cancer and inflammation. Their involvement in crucial pathologies makes them interesting targets for drug discovery. In this review, we gather the last approaches toward the specific design of glycomimetics as potential drugs against galectins. Different approaches, either using specific glycomimetic molecules decorated with key functional groups or employing multivalent presentations of lactose and N-acetyl lactosamine analogs, have provided promising results for binding and modulating different galectins. The review highlights the results obtained with these approximations, from the employment of S-glycosyl compounds to peptidomimetics and multivalent glycopolymers, mostly employed to recognize and/or detecthGal-1 andhGal-3. |
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