Open AccessCOVID-19 Protease Inhibitor using Azole N-Mannich Bases: A Molecular Docking Approach
Author(s) -
K.N. Arathi,
K. Abdul Khayum,
Sulaiman Mohammed Alnasser,
Onsinyo James Meroka
Publication year - 2021
Publication title -
asian journal of chemistry/asian journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.145
H-Index - 34
eISSN - 0975-427X
pISSN - 0970-7077
DOI - 10.14233/ajchem.2021.23100
Subject(s) - autodock , chemistry , docking (animal) , protease , stereochemistry , moiety , protein data bank (rcsb pdb) , mannich base , piperazine , azole , active site , enzyme , combinatorial chemistry , biochemistry , organic chemistry , in silico , biology , medicine , antifungal , nursing , microbiology and biotechnology , gene
Coronaviruses are the largest group of viruses belonging to the Nidovirales order, which includesCoronaviridae, Arteriviridae and Roniviridae families. In this work, a molecular modeling techniqueis adopted to find out the excellent moiety to inhibit the protease enzyme which is present in thecoronavirus. Autodock 4.2 tool was used to find out the docking score of 32 ligands. The molinspirationserver helps to find out the drug-likeness property and whether these ligands having a binding towardsthe protease enzyme. The synthetic N-Mannich bases of azole were docked with COVID-19 mainprotease in complex with an inhibitor N3 (PDB id: 6lu7). Among 32 ligand molecules, around 25ligands showed an excellent binding score when compared to the standard drug favipiravir. The presenceof dimethyl group in the pyrazole nucleus helps good interaction with protease enzyme. Among theMannich bases, the secondary amine mannich base of piperazine considered as the best derivative toinhibit the protease enzyme.