Connecting simulated, bioanalytical, and molecular docking data on the stereoselective binding of (±)-catechin to human serum albumin.
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.
Department of Chemistry, Durban University of Technology, PO Box 1334, Durban 4000, South Africa.
Myalowenkosy I
MI
Sabela
Njabulo J
NJ
Gumede
Laura
L
Escuder-Gilabert
Yolanda
Y
Martín-Biosca
Khirsna
K
Bisetty
María-Jose
MJ
Medina-Hernández
Salvador
S
Sagrado
D001665:Binding Sites; D002392:Catechin / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D008962:Models, Theoretical; D056004:Molecular Dynamics Simulation; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism*; D013237:Stereoisomerism; D014462:Ultrafiltration
D012709:Serum Albumin; D002392:Catechin