Insilico and Invitro Evaluation of Dy(III) Complex on Serum Albumin as well as Amino Acid Loops in M-Protease of SARS-Coronavirus-2

Countless proteins contain signal patterns that act as entry point and guiding others protein to particular cell frameworks. Likewise, the mutation in the main chain protease of “spike” proteins seemed to be crucial in viral infection and recombination in COVID-19. A certain drug that binds to the sequence will further prevent coronavirus synchronization. To address this, we designed and characterized a new complex for COVID-19 inhibition that contains 1,10-phenantroline as a ligand and Dy(III) as more than just a metal. The absorption character in neat solvent, in the existence of 4.5 percent BSA, as well as the biological interplay of COVID-19 virus via molecular docking, has been carried out to determine the complex's efficacy in this pandemic situation. The complex's absorbance spectra shows intense peaks that correspond to intra ligand π - π*, n - π*, and charge transfer transitions. It also shows a red shift in peaks corresponding to LCT and MLCT transitions in 4.5 percent of BSA. The molecular docking analysis of the complex with the COVID-19 virus (PDB: 6LU7) reveals a strong polar interaction with various amino acids in the spike protein. The complex has awesome binding energies in the -8.8 kcal mol-1 range. As a result, they are legit contender compounds for the development of candidates against SARS-COV-2. We also evaluated the complex's basic energies, such as potential and steric energy, using Gaussian energy calculations.