Virtual Screening of a Series of Phytocompounds from Polygonum cuspidatum for Identification of Potential Antibacterial Drug Candidates: an In-silico and Drug Design Approaches

ABSTRACT

In recent times, the emergence of Clostridium perfringens has posed a significant challenge to public health due to its antibiotic resistance and the formation of biofilms. It is the neuraminidase enzyme that supplies toxin secretion from C. perfringens. Since the sialic acid bond is a target recognition point for bacteria, new molecules are needed to treat infections caused by dangerous pathogens such as C. perfringens.The present work focused on an alternative strategy using compounds from Polygonum cuspidatum Sieb. et Zucc. Nine bioactive compounds derived from this plant emodin, physcion, emodin-1-O-β-D-glucopyranoside, emodin-8-O-β-D-glucopyranoside, physcion-8-O-β-D-glucopyranoside, 2-methoxy-6-acetyl-7-methyl juglone, torachrysone-8-O-β-D-glucoside, polydatin and resveratrol were used as ligands and coupled. The neuraminidase enzyme from C. perfringens was chosen as the target protein. The optimal ligand insertion score and ADMET parameters were determined by employing the Lipinski rules as selection criteria. Emodin-8-O-β-D-glucopyranoside and physcion-8-O-β-D-glucopyranoside exhibited drug-like characteristics in their ability to inhibit neuraminidase, as evidenced by a chelation score of −11.9. A comparison was conducted between emodin-8-O-β-D-glucopyranoside and physcion-8-O-β-D-glucopyranoside, and the positive control quercetin.A comprehensive analysis of the drug-like properties of emodin-8-O-β-D-glucopyranoside and physcion-8-O-β-D-glucopyranoside revealed that exhibited superiority over quercetin across multiple aspects. Quercetin showed a binding affinity of −9.9, while emodin-8-O-β-D-glucopyranoside and physcion-8-O-β-D-glucopyranoside showed a binding affinity of −11.9. The results showed acceptable differential kinetic properties of emodin-8-O-β-D-glucopyranoside and physcion-8-O-β-D-glucopyranoside compared to quercetin. It has been shown to inhibit the neuraminidase enzyme from C. perfringens.