Connecting simulated, bioanalytical, and molecular docking data on the stereoselective binding of (±)-catechin to human serum albumin
| Autor: | Yolanda Martín-Biosca, Njabulo J. Gumede, Laura Escuder-Gilabert, Myalowenkosy I. Sabela, Salvador Sagrado, Khirsna Bisetty, M.J. Medina-Hernández |
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| Rok vydání: | 2011 |
| Předmět: |
Models
Molecular Bioanalysis Serum albumin Ultrafiltration Stereoisomerism Plasma protein binding Molecular Dynamics Simulation Biochemistry Catechin Analytical Chemistry medicine Humans Binding site Serum Albumin Binding Sites Chromatography biology Chemistry Models Theoretical Human serum albumin body regions biology.protein Stereoselectivity Enantiomer Protein Binding medicine.drug |
| Zdroj: | Analytical and Bioanalytical Chemistry. 402:1899-1909 |
| ISSN: | 1618-2650 1618-2642 |
| DOI: | 10.1007/s00216-011-5636-5 |
| Popis: | The stereoselective binding of the frequently ingested nutraceutical (±)-catechin, with demonstrated differential biological activity between enantiomers, to human serum albumin (HSA), with the largest complexation and enantioselectivity potential among the plasmatic proteins, is studied by combining simulations to optimize the experimental design, robust in vitro electrokinetic chromatographic data, and molecular docking-chiral recognition estimates. Methodological and mathematical drawbacks in previous reports on (±)-catechin-HSA are detected and eliminated. Recent and novel direct equations extracted from the classical interaction model allows advantageous univariate mathematical data treatment, providing the first evidence of quantitative (±)-catechin-HSA enantioselectivity. Also, the binding site in HSA of the enantiomers is approached, and both the experimental enantioselectivity and the main binding site information are contrasted with a molecular docking approach. |
| Databáze: | OpenAIRE |
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