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

• DOI: 10.24018/ejchem.2023.4.3.140
• Publication Date: 2023-05-09T09:29:44Z
• Authors: Daniel Hassan Mhya; Abdulrashid Mohammed; Theophilus Tagun ...
• Keywords: Docking (animal); Gallate; Apocynin

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.