Binding interaction of atorvastatin with bovine serum albumin: Spectroscopic methods and molecular docking

• Atorvastatin binds to the subdomain IIA (site I) of BSA and forms 1:1 complex with it.
• The fluorescence quenching of BSA induced by atorvastatin is a combined dynamic and static quenching.
• Atorvastatin binding results in a decrease in α-helix content of BSA.
• The main interaction forces are van der Waals and hydrogen bonding interactions.
• The flexibility of atorvastatin plays an important role in increasing the atorvastatin–BSA stability.

The interaction of atorvastatin with bovine serum albumin (BSA) was investigated using multi-spectroscopic methods and molecular docking technique for providing important insight into further elucidating the store and transport process of atorvastatin in the body and the mechanism of action and pharmacokinetics. The experimental results revealed that the fluorescence quenching mechanism of BSA induced atorvastatin was a combined dynamic and static quenching. The binding constant and number of binding site of atorvastatin with BSA under simulated physiological conditions (pH = 7.4) were 1.41 × 105 M− 1 and about 1 at 310 K, respectively. The values of the enthalpic change (ΔH0), entropic change (ΔS0) and Gibbs free energy (ΔG0) in the binding process of atorvastatin with BSA at 310 K were negative, suggesting that the binding process of atorvastatin and BSA was spontaneous and the main interaction forces were van der Waals force and hydrogen bonding interaction. Moreover, atorvastatin was bound into the subdomain IIA (site I) of BSA, resulting in a slight change of the conformation of BSA.

It was confirmed that atorvastatin binds to site I of BSA via van der Waals and hydrogen bonding interactions and forms 1:1 complex with it through spectroscopic methods and molecular docking.Figure optionsDownload as PowerPoint slide