Structural insights into the binding behavior of flavonoids naringenin with Human Serum Albumin

Abstract

The natural polyphenolic compounds present in fruits, vegetables, nuts, and tea are flavonoids. naringenin is one of the most critical flavonoids derivative in certain eatable fruits, such as citrus. Human Serum albumin (HSA) is a protein that is widely used as a bearer for drug binding studies. The spectroscopic and computational methods were employed in this analysis to peruse the efficacy of naringenin on the HSA structure. Analysis of fluorescence demonstrated the static quenching mechanism. Results from the different experiments have shown that naringenin binds to HSA. At three temperatures, the binding constant, the number of binding sites, and temperature parameters (somewhere between ΔH°, somewhere between ΔS°, and somewhere between ΔG°) were calculated. The experiences of Van der Waals and bonding hydrogen were considered to be the main forces. The results of molecular dynamics simulation and thermal denaturation show that naringenin increases the stability of HSA and decreases its flexibility. Due to the decline in the gyration radius (Rg) in attendance of naringenin, protein is more folded. The amount of RMSD decreases in the presence of naringenin, indicating which HSA becomes more stable by binding to naringenin. The mean RMSF of free HSA in the presence of naringenin demonstrated a decrease in protein flexibility during the simulation. ASA values show that most of the Trp and Tyr residues moved outward from the protein (more polar medium).