Investigation of the Several Aspects of Interaction between Human Serum Albumin and Oleic Acid by Molecular Dynamic Simulation Approaches and Spectroscopic Methods

Abstract

The most predominant fatty acid in olive oil, oleic acid (OA), lowers LDL (low-density lipoprotein) cholesterol and may raise HDL (high-density lipoprotein cholesterol). As a result, it effectively improves heart function and prevents heart diseases. In the current research, the OA interaction with HSA (human serum albumin) was evaluated by spectroscopic and computational modeling methods to determine the impact of OA on the body. Observations from the absorption spectra proved the complexation of HSA with OA. An enhancement in the fluorescence intensity shows that interactions between HSA and OA have altered the milieu enclosing the fluorophore and altered the structures of HSA. Van der Waals forces and hydrogen bonds were determined to be the main factors producing the HSA-OA complex by molecular docking. The HSA structure’s α-helix was decreased, as per evidence of far-UV CD spectroscopy. The activity of HSA represented OA binding with HSA in a competitive mode. Investigation of the esterase activity of HSA reveals that OA could inhibit its activity. The information obtained from the MD (Molecular dynamics) simulation proved that the binding of the OA causes stability in the HSA structure, and the structure of the HSA becomes more compact by OA binding and reduces the flexibility of the residues. The data obtained in the present work improves our understanding of the activity and mechanism of binding and provides a valuable experimental approach for investigating the OA-HSA compound.