The well-defined and characterized 3D crystal structure of a protein is important to explore the topological and physiological features of the protein. The distinguished topography of a protein helps medical chemists design drugs on the basis of the pharmacophoric features of the protein. Structure-based drug discovery, specifically for pathological proteins that cause a higher risk of disease, takes advantage of this fact. Current tools for studying drug-protein interactions include physical, chromatographic, and electrophoretic methods. These techniques can be separated into either non-spectroscopic (equilibrium dialysis, ultrafiltration, ultracentrifugation, etc.) or spectroscopic (Fluorescence spectroscopy, NMR, X-ray diffraction, etc.) methods. These methods, however, can be time-consuming and expensive. On the other hand, in silico methods of analyzing protein-drug interactions, such as docking, molecular simulations, and High-Throughput Virtual Screenings (HTVS), are heavily underutilized by core drug discovery laboratories. These kinds of approaches have a great potential for the mass screening of potential small drugs molecules. Studying protein-drug interactions is of particular importance for understanding how the structural conformation of protein elements affect overall ligand binding affinity. By taking a bioinformatics approach to analyzing drug-protein interactions, the speed with which we identify potential drugs for genetic targets can be greatly increased.
Keywords: Drug discovery; High-Throughput Virtual Screenings; Protein Drug interaction.