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논문 기본 정보

자료유형
학술저널
저자정보
Sultan Mehtap Büyüker (Üsküdar University Çarşı Campus) Syed Babar Jamal (National University of Medical Sciences) Sumra Wajid Abbasi (National University of Medical Sciences) Muhammad Faheem (University of North Dakota) Shah Jahan (University of Peshawar)
저널정보
한국생약학회 Natural Product Sciences Natural Product Sciences Vol.30 No.2
발행연도
2024.6
수록면
148 - 160 (13page)
DOI
10.20307/nps.2024.30.2.148

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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.
#Pharmacokinetics #Multidrug resistance #Molecular docking #Polygonum cuspidatum #Clostridium perfringens #Quercetin

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Abstract
Introduction
Materials and Methods
Results and Discussion
References

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