Molecular Docking Study of Pyrazole Interaction with Bovine Serum Albumin (BSA): Insights from Drug -Protein Binding

The interaction of drugs with plasma proteins, especially Bovine Serum Albumin (BSA), affects the half-life and biological activity of the drug. Serum albumins, due to their abundance, flexibility, and ability to bind to both hydrophilic and hydrophobic groups, are responsible for key functions such as maintaining blood pH and osmotic pressure, as well as transporting various substances including fatty acids, steroids, hormones, amino acids, metal ions, carbohydrates, and other molecules throughout the bloodstream, both intracellularly and extracellularly. Bovine Serum Albumin is used as a model to study these types of interactions due to its high structural similarity to Human Serum Albumin (HAS). Pyrazole has been considered as an important active pharmaceutical scaffold with high potential in various pharmaceutical fields. This study investigates the interaction of pyrazole with BSA using the molecular docking method. The aim of this study was to better understand the binding of drug to albumin and its effect on the biological activity of the drug, as well as, to investigate the medicinal potential of pyrazole and its derivatives. Three-dimensional (۳D) structure of the ligand and BSA(۴F۵S) were obtained from the PubChem database and Protein Data Bank (PDB), respectively. Finally, the molecular docking was studied using Autodock ۴.۱ software. Analysis of the molecular docking exhibited that Pyrazole interacts with the B chain of the protein with the binding energy of -۳.۳۷ kcal/mol. As results showed, pyrazole binds to BSA protein, and therefore, it may affect the protein interior interactions.

کلیدواژه ها:

Bovine Serum Albumin (BSA) ، protein ، Pyrazole ، molecular docking