Study of the interaction of Crizotinib with serum albumin protein by functional density theory method

Anticancer medicine Crizotinib is considered as one of the most important inhibitors of lung cancer tumors. This drug prevents the proliferation of cancer cells through the mechanism of inhibiting ROS1 and ALK activity. Human serum albumin is commonly used as a protein pattern is used to describe a protein-drug complex.Albumin is the only protein in the body capable of binding to a wide range of high-potency and reversible high-density ligands. In this study, the association of Crizotinib anticancer drug with human albumin serum protein by functional density theory The molecular perspective was studied. In this study, the iGEMDOCK drug-protein complex was first prepared by Docking software, then calculations of the density functional theory were performed by Gaussian 09 software.The density functional theory showed that the energy difference between two orbital HOMO and LUMO for Crizotinib before and after transplantation was 1.48 and 0.84 units respectively. Some of the amino acids involved in binding to Crizotinib include tryptophan 21, serine 202, and phenylalanine 212 The drug is much more reactive and stable than the free drug at the site of protein binding. Regarding the electron deployment diagram obtained from the analysis of the supercomputer, the six-membered rings of Crizotinib have the greatest tendency to have albumin-based serum protein structure

کلیدواژه ها:

Cancer ، Quantum Mechanics ، Crizotinib ، Albumin