EXPLORATION OF ALOE-EMODIN DERIVATIVES AS POTENTIAL SUCCINATE DEHYDROGENASE INHIBITORS VIA COMPUTATIONAL SIMULATION STUDIES

Abstract

 Succinate dehydrogenase (SDH) is a crucial target for controlling and inhibiting various plant pathogenic fungi. In this study, a dataset of 32 compounds was designed based on the aloe-emodin scaffold. Computational simulations were performed to predict interactions between these compounds and SDH (PDB ID: 2FBW). The results indicated that the compounds exhibited strong interactions with the amino acids at the SDH active site. The predicted binding energies were all lower than -6.0 kcal/mol, while the binding energy of carboxin (the reference compound) was -6.5 kcal/mol. In particular, derivative 05 (3-methyl-9,10-dioxo-9,10-dihydroanthracene-1,8-diyl dibenzoate) had the lowest predicted binding energy of -10.5 kcal/mol, which is a 4 kcal/mol difference compared to carboxin. Therefore, this compound is considered a potential candidate for future synthesis and bioactivity evaluation studies.