Connecting simulated, bioanalytical, and molecular docking data on the stereoselective binding of (卤)-catechin to human serum albumin

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• 作者：Myalowenkosy I. Sabela (1)
  Njabulo J. Gumede (2)
  Laura Escuder-Gilabert (3)
  Yolanda Mart铆n-Biosca (3)
  Khirsna Bisetty (1)
  Mar铆a-Jose Medina-Hern谩ndez (3)
  Salvador Sagrado (34) sagrado@uv.es
• 关键词：Stereoselective protein&#8211 ; ligand binding &#8211 ; Electrokinetic chromatography &#8211 ; Molecular docking&#8211 ; chiral recognition &#8211 ; Catechin &#8211 ; Human serum albumin
• 刊名：Analytical and Bioanalytical Chemistry
• 出版时间：February 2012
• 出版年：2012
• 期刊代码：8_1618-2642
• 类别：en
• 卷：402
• 期：5
• 页码：1899-1909
• 数据来源：sp

摘要

The stereoselective binding of the frequently ingested nutraceutical (卤)-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 (卤)-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 (卤)-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.