ArticleChemistry, an Asian journal2007
Thermodynamic parameters for the association of fluorinated benzenesulfonamides with bovine carbonic anhydrase II.
Article in Chemistry, an Asian journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 58 citations in OpenAlex.
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- Structure and mechanism of secondary sulfonamide binding to carbonic anhydrases.European biophysics journal : EBJ · 2021Article
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- Optimization of Acetazolamide-Based Scaffold as Potent Inhibitors of Vancomycin-ResistantJournal of medicinal chemistry · 2020Article
- The Influence of Varying Fluorination Patterns on the Thermodynamics and Kinetics of Benzenesulfonamide Binding to Human Carbonic Anhydrase II.Biomolecules · 2020Article
- Novel fluorinated carbonic anhydrase IX inhibitors reduce hypoxia-induced acidification and clonogenic survival of cancer cells.Oncotarget · 2018Article
- Cross-strand interactions of fluorinated amino acids in β-hairpin constructs.Journal of the American Chemical Society · 2012Article
- Fluoroalkyl and alkyl chains have similar hydrophobicities in binding to the "hydrophobic wall" of carbonic anhydrase.Journal of the American Chemical Society · 2011Article
- Synthesis of novel aryl(heteroaryl)sulfonyl ureas of possible biological interest.Molecules (Basel, Switzerland) · 2010Article
- Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.Chemical reviews · 2008Review
- Dependence of effective molarity on linker length for an intramolecular protein-ligand system.Journal of the American Chemical Society · 2007Article
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
This paper describes a calorimetric study of the association of a series of seven fluorinated benzenesulfonamide ligands (C6H(n)F(5-n)SO2NH2) with bovine carbonic anhydrase II (BCA). Quantitative structure-activity relationships between the free energy, enthalpy, and entropy of binding and pKa and log P of the ligands allowed the evaluation of the thermodynamic parameters in terms of the two independent effects of fluorination on the ligand: its electrostatic potential and its hydrophobicity. The parameters were partitioned to the three different structural interactions between the ligand and BCA: the Zn(II) cofactor-sulfonamide bond (approximately 65% of the free energy of binding), the hydrogen bonds between the ligand and BCA (approximately 10%), and the contacts between the phenyl ring of the ligand and BCA (approximately 25%). Calorimetry revealed that all of the ligands studied bind in a 1:1 stoichiometry with BCA; this result was confirmed by 19F NMR spectroscopy and X-ray crystallography (for complexes with human carbonic anhydrase II).
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