Tianeptine Esters Derivatives: A Study of Protein-Drug Interaction Performed by Fluorescence Quenching and Molecular Docking

Abstract

The nature of binding between bovine serum albumin (BSA) and the antidepressant tianeptine and a new series of esters derivatives were studied in this paper. The interactions with BSA were investigated by UV-Vis and fluorescence spectroscopy at three different temperatures. The fluorescence quenching experiments showed that BSA interactions with tianeptine could be dynamic while to its esters a static mechanism was observed. The results showed that tianeptine quenches the intrinsic fluorescence of BSA more efficiently than its esters due to the presence of the free acid portion. The number of binding sites determined by fluorescence spectroscopy is approximately equal to 1 indicating that there is one binding site between BSA tianeptine esters, but the presence of a second interaction site for tianeptine at higher temperatures could be not ruled out. Molecular docking calculations point out a strong affinity of tianeptine and its esters to the site IIA of protein, supporting the hypothesis of a static quenching mechanism.

Quinoline Functionalized Schiff Base Silver (I) Complexes: Interactions with Biomolecules and In Vitro Cytotoxicity, Antioxidant and Antimicrobial Activities

“…Complex Q12 had the highest binding affinity ( Figure 6 a), followed by Q4 ( Figure S60 ) and Q15 ( Figure S70 ). The influence of Q4 , Q12 , and Q15 ligand substituents on their binding affinity to BSA can be related to similar literature reports [ 87 , 88 , 89 ]. The order of binding constant for the complexes is: Q12 > Q15 > Q4 > Q8 > Q7 > Q11 > Q10 > Q2 > Q14 > Q5 > Q6 > Q9 > Q3 > Q1 > Q13 .…”