ArticlePharmaceuticals (Basel, Switzerland)2020
Binding Constants of Substituted Benzoic Acids with Bovine Serum Albumin.
Article in Pharmaceuticals (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 16 citations in OpenAlex.
- Photophysical Properties and Protein Binding Studies of Piperazine-Substituted Anthracene-BODIPY Dyads for Antimicrobial Photodynamic Therapy.Molecules (Basel, Switzerland) · 2025Article
- Adsorption and Morphology Analysis of Bovine Serum Albumin on a Micropillar-Enhanced Quartz Crystal Microbalance.The journal of physical chemistry. B · 2024Article
- Calix[4]Resorcinarene Carboxybetaines and Carboxybetaine Esters: Synthesis, Investigation of In Vitro Toxicity, Anti-Platelet Effects, Anticoagulant Activity, and BSA Binding Affinities.International journal of molecular sciences · 2022Article
- Biogenic Ferrihydrite Nanoparticles Produced byNanomaterials (Basel, Switzerland) · 2022Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Experimental data on the affinity of various substances to albumin are essential for the development of empirical models to predict plasma binding of drug candidates. Binding of 24 substituted benzoic acid anions to bovine serum albumin was studied using spectrofluorimetric titration. The equilibrium constants of binding at 298 K were determined according to 1:1 complex formation model. The relationships between the ligand structure and albumin affinity are analyzed. The binding constant values for m- and p-monosubstituted acids show a good correlation with the Hammett constants of substituents. Two- and three-parameter quantitative structure-activity relationship (QSAR) models with theoretical molecular descriptors are able to satisfactorily describe the obtained values for the whole set of acids. It is shown that the electron-density distribution in the aromatic ring exerts crucial influence on the albumin affinity.
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