Evidence for CCl/CBr⋅⋅⋅π Interactions as an Important Contribution to Protein-Ligand Binding Affinity
| Autor: | Armin Bauer, Volkmar Wehner, Marc Nazaré, Hans Matter, Michael Wagner, Herman Schreuder, Stefan Güssregen, Matthias Urmann, Kurt Ritter, David William Will |
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| Rok vydání: | 2009 |
| Předmět: |
Bromides
Indoles medicine.drug_mechanism_of_action Stereochemistry Factor Xa Inhibitor Electrons Crystallography X-Ray Catalysis Structure-Activity Relationship Molecular recognition polycyclic compounds medicine Non-covalent interactions Structure–activity relationship Pi interaction Binding site chemistry.chemical_classification Binding Sites Aromaticity General Chemistry General Medicine chemistry Factor Xa Thermodynamics Tyrosine Chlorine Factor Xa Inhibitors Protein Binding Protein ligand |
| Zdroj: | Angewandte Chemie. 121:2955-2960 |
| ISSN: | 0044-8249 |
| DOI: | 10.1002/ange.200806219 |
| Popis: | Attractive chlorine: Noncovalent interactions between chlorine or bromine atoms and aromatic rings in proteins open up a new method for the manipulation of molecular recognition. Substitution at distinct positions of two factor Xa inhibitors improves the free energy of binding by interaction with a tyrosine unit. The generality of this motif was underscored by multiple crystal structures as well as high-level quantum chemical calculations (see picture). |
| Databáze: | OpenAIRE |
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