Investigation of the anti-cancer drugs imatinib and thalidomide using analytical spectroscopy (FT-IR, UV-Vis) and molecular docking simulations

Abstract

Cancer is one of the most fatal diseases in modern civilisation, accounting for a significant number of deaths each year. The continued investigation of the medical effects of cancer is still an important and fascinating field of study. Imatinib and Thalidomide are important anti-cancer drugs that are not thoroughly studied or have molecular docking studies to obtain one-on-one drug-protein interactions, which is crucial information. The research in this important study focuses on exploring specific vibrational patterns of these drugs using standard experimental FT-IR and UV-Vis spectroscopic studies and molecular docking computations. The study effectively identified specific atomic-level interactions between the malignant medication Thalidomide and the protein Cereblon isoform 4 and the anti-cancer treatment Imatinib and the target proteins, especially Tyrosine kinase Sh2 domain and Tyrosine-protein kinase ABL1. The UV-Vis spectra of the medications were examined in order to comprehend the bioactivity of the molecule and the charge transfer between its outermost orbitals. The accurate energy gaps were evaluated using energy-wavelength conversions based on quantum mechanics. Important details such as binding affinity, RMSD (Root Mean Square Deviation), the kinds of interactions formed, and the unique pathways that the agent and receptors have developed were revealed by the molecular docking studies involving imatinib and thalidomide and the corresponding binding proteins. The molecular docking studies for imatinib and thalidomide were conducted utilising the target proteins Tyrosine kinase Sh2 domain, Tyrosine-protein kinase ABL1, and Cereblon isoform 4 protein, using the programs AutoDock 1.5.6 and BIOVIA. The numerous types of one-to-one bindings between specific atoms, protein epitope groups, and the ligand were tabulated, and it was shown that ligand-protein Pose-1 and Pose-2 of Tyrosine kinase Sh2 domain, Tyrosine-protein kinase ABL1, and Cereblon isoform 4 protein binding interactions had binding affinity values of -8.2 and -8.2 kcal-mole^-1, -10.1 and -11 kcal-mole^-1, and -6.3 and -6.2 kcal-mole^-1, respectively. These findings made in understanding the behaviour of anticancer drugs are significant additions to our growing knowledge of the subject. These discoveries not only improve the effectiveness of already available therapies but also significantly influence the advancement of innovative anticancer medications.