Abstract
Abstract The interaction between pentoxifylline (PTX) and bovine serum albumin (BSA) was studied under physiological condition by spectroscopic, voltammetry and molecular modelling techniques. The results of fluorescence studies revealed that the quenching mechanism of BSA by PTX was a static procedure. Binding constant of PTX-BSA was calculated and its value found to be 8.895 × 104 M−1, which is in close agreement with the results obtained from UV-Visible and voltammetry approach. The negative values of thermodynamic parameters (ΔG, ΔH and ΔS) indicated that van der Waals force and hydrogen bonding play major roles in the interaction of PTX with BSA. Based on Forster’s theory of non-radiation energy transfer, the binding distance (r) between the donor (BSA) and acceptor (PTX) was found to be 5.38 nm (298 K). The results of UV-Visible and circular dichroism (CD) spectroscopy showed that PTX interacts with BSA and induces conformational changes by reducing the α-helix content. The results of the UV-visible and voltammetry studies were further verified by the molecular docking method. Molecular modelling studies revealed possible residues involved in the drug-protein interaction and indicated that PTX binds to Site IIA of BSA.
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