Synthesis, characterization, DFT studies, and molecular modeling of azo dye derivatives as potential candidate for trypanosomiasis treatment

•This research aims to synthesize four compounds (CMP1, CMP2, CMP3 and CMP4) have been spectroscopically analyzed using UV–vis and FT-IR techniques.•The HOMO-LUMO energy analysis indicate that CMP4 possesses the largest energy gap of 3.327 eV.•CMP1 showed its highest stabilization energy with of 1243.14 kcal/mol, CMP2 at 47,120.45 kcal/mol, CMP3 at 694.91 kcal/mol, and CMP4 at 9471.63 kcal/mol.•All ligands exhibited higher binding affinities with 3ICK and 5QQ5 which suggest formation of stable complex with this protein compared to the standard drug.•Molecular docking investigation indicates that the compounds have bioactivity towards vector-borne parasitic disease caused by Trypanosoma cruzi. This research aims to synthesize four compounds (CMP1, CMP2, CMP3 and CMP4) and determine their suitability for the formulation of the drugs for the treatment of sleeping sickness caused by Trypanosoma cruzi, a vector-borne parasitic disease, commonly referred to as sleeping sickness. The synthesized azo dyes have been spectroscopically analyzed using UV–vis and FT-IR techniques along with detailed functional groups comparison through vibrational assignment. All theoretical computation was carried out within the framework of density functional theory (DFT) at the B3LYP/ 6–311++G(d) method and molecular properties such as frontier molecular orbital (FMO), natural bond orbital (NBO), nonlinear optics (NLO), condensed fukui function, and Total density of state (TDOS) have been evaluated. The results of the HOMO-LUMO energy analysis indicate that CMP4 possesses the largest energy gap of 3.327 eV compared to the rest of the compounds and has the highest stability. For the NBO analysis, CMP1 showed its highest stabilization energy with of 1243.14 kcal/mol, CMP2 at 47,120.45 kcal/mol, CMP3 at 694.91 kcal/mol, and CMP4 at 9471.63 kcal/mol. NLO shows CMP2 with the highest dipole moment of 10.59D and CMP1 with the lowest dipole moment of 2.5435D. All ligands exhibited higher binding affinities with 3ick and 5qq5 which suggest formation of stable complex with this protein compared to the standard drug. Therefore, molecular electronic structure and molecular docking investigation indicates that the azo compounds have unique reactivity and bioactivity towards vector-borne parasitic disease caused by Trypanosoma cruzi. [Display omitted]