Monovalent and bivalent N-fucosyl amides as high affinity ligands for Pseudomonas aeruginosa PA-IIL lectin
| العنوان: | Monovalent and bivalent N-fucosyl amides as high affinity ligands for Pseudomonas aeruginosa PA-IIL lectin |
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| المؤلفون: | Aymeric Audfray, Anne Imberty, Manuel Andreini, Marko Anderluh, Anna Bernardi |
| المساهمون: | inconnu, Inconnu, Centre de Recherches sur les Macromolécules Végétales (CERMAV), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF) |
| المصدر: | Carbohydrate Research Carbohydrate Research, Elsevier, 2010, pp.1400-1407 |
| بيانات النشر: | Elsevier BV, 2010. |
| سنة النشر: | 2010 |
| مصطلحات موضوعية: | Models, Molecular, Glycosylation, Protein Conformation, Glycoconjugate, Stereochemistry, Ligands, Biochemistry, Analytical Chemistry, Divalent, chemistry.chemical_compound, Glycomimetic, Lectins, Amide, Adhesins, Bacterial, ComputingMilieux_MISCELLANEOUS, Fucose, chemistry.chemical_classification, biology, Ligand, Organic Chemistry, Lectin, General Medicine, Amides, Aglycone, chemistry, Pseudomonas aeruginosa, biology.protein, Protein Binding |
| الوصف: | The adhesion of bacteria to human glycoconjugates can be inhibited by soluble glycomimetics that compete with the natural target. Four monovalent and one divalent alpha-fucosyl amides have been tested for their affinity for a fucose-binding lectin from Pseudomonas aeruginosa. Isothermal calorimetric titrations demonstrated that they bind to the lectin in the micromolar range, with highest affinity for the divalent ligand. Molecular modelling established that, compared to Omicron-fucoside compounds, the glycomimetic amide group resulted in the loss of water-bridged hydrogen bonds that could be partially compensated by additional contact of the aglycone with the protein surface. |
| تدمد: | 0008-6215 |
| DOI: | 10.1016/j.carres.2010.03.012 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1dce6e3633e1ce63536002b293210cf5 https://doi.org/10.1016/j.carres.2010.03.012 |
| Rights: | CLOSED |
| رقم الانضمام: | edsair.doi.dedup.....1dce6e3633e1ce63536002b293210cf5 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 00086215 |
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| DOI: | 10.1016/j.carres.2010.03.012 |