Investigation of NADPH-Oxidase’s Binding Subunit(s) for Catechin Compounds Induce Inhibition

Catechins are natural polyphenolic compounds with ability to minimize excess free radicals through different mechanisms including inhibition of NADPH oxidase (NOX) activity. NOX is a complex enzyme made-up several subunits, where molecules catechins binds exert their effect. Hence, the attempt probe enzyme’s binding subunit catechins-induce Several in-silico techniques were deployed in probing catechins. The downloaded from PubChem database SDF files. five subunits PDB ID: 3A1F, 1OV3, 1HH4, 1OEY, and 7CFZ protein databank. Drug-likeness properties biological activities predicted using ADMETMESH software. Catechin-NOX subunits’ interactions was performed via molecular docking, docked conformations analyzed Protein-plus results study catechin compounds; epicatechin (E), gallate (EG) epigallocatehin (EGG) drug-like nature possess enzymes inhibitory properties. Docking result capable interacting various but varied degree. Their (catechins) strongest affinities on p40phox p67phox PB1 (PBD: 1OEY) energies ranges -8.3 -9.9kcal/mol this order; Apocynin>EGG>EG>E. While weak affinity between gp91 (phox) (PDB: 3A1F) (-4.9 -6.5 kcal/mol) sequence; E<apocynin<EGG<EG. In conclusion, drug-likeness has for interaction NADPH-oxidase particularly probably antioxidant effects. Therefore, vitro vivo recommended verify claim.