The effect of Pseudomonas fluorescens biosurfactant pseudofactin II on the conformational changes of bovine serum albumin: Pharmaceutical and biomedical applications

Herein, we have investigated the binding interaction of bovine serum albumin (BSA) with a biosurfactant pseudofactin II (PF) in physiological buffer medium through the use of surface tension, fluorescence, circular dichroism (CD), isothermal titration calorimetry (ITC) and molecular docking studies. Fluorescence results showed that PF interacts with BSA through a static quenching mechanism. CD results demonstrate a conformational change in BSA upon PF combination. The negative Gibbs free energies obtained through ITC experiment suggest that the binding process is spontaneous. Molecular docking further provides an insight of various residues that are involved in this binding process, showing a binding energy of −58.6 kcal mol−1. The present study will help understand the binding mechanism of lipopeptide biosurfactant (PF) to proteins as well as the associated stability and conformational changes.