Interaction of Milk α- and β-Caseins with Atorvastatin: Spectroscopic Methods and Molecular Docking Approach

Throughout this research the interaction between α- and β-caseins with atorvastatin was explored at physiological conditions, using fixed protein concentration and various atorvastatin contents. FTIR, UV‒visible and fluorescence spectroscopic methods as well as molecular modeling were used to analyz...

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Bibliographic Details
Published in:Russian Journal of Physical Chemistry A 2023-06, Vol.97 (6), p.1245-1252
Main Authors: Dezhampanah, Hamid, Miandehi, Omideh Rajabi
Format: Article
Language:English
Subjects:
Binding sites
Casein
Chemistry
Chemistry and Materials Science
Chemoinformatics and Computer Modeling
Energy transfer
Fluorescence
Fourier transforms
Hydrogen bonds
Infrared spectroscopy
Molecular docking
Physical Chemistry
Physiology
Proteins
Stability analysis
Structural analysis
Structural stability
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Summary:Throughout this research the interaction between α- and β-caseins with atorvastatin was explored at physiological conditions, using fixed protein concentration and various atorvastatin contents. FTIR, UV‒visible and fluorescence spectroscopic methods as well as molecular modeling were used to analyze atorvastatin binding sites, binding constant and the effect of atorvastatin interaction on the stability and secondary structure of caseins. Structural analysis indicated that overall binding constants values of 3.92 × 10 4 and 0.94 × 10 4 M –1 for atorvastatin-α-casein and atorvastatin-β-casein complexes, respectively with single binding site for atorvastatin via located on the surface of the protein molecule under simulated physiological conditions. The distances between the α-casein and β-casein as the donor and atorvastatin as the receptor were determined by Fӧrster resonance energy transfer showed that atorvastatin binds to the Trp residues of α- and β-caseins molecules with short distances. Docking study showed that atorvastatin molecule made several hydrogen bonds and van der Waals interactions with α- and β-caseins. The results of UV–Vis absorption, synchronous fluorescence and FT-IR spectra demonstrated that caseins interact with atorvastatin molecule mainly via hydrophobic and hydrophilic interactions and the secondary structure of caseins are changed.
ISSN:0036-0244
1531-863X
DOI:10.1134/S0036024423060055