数量结构-活动关系
唑
对接(动物)
化学
多奈哌齐
生物信息学
分子动力学
厕所
立体化学
乙酰胆碱酯酶
计算化学
计算生物学
生物化学
酶
抗真菌
生物
医学
护理部
微生物学
痴呆
疾病
病理
基因
作者
Kajal Gupta,Akshay Kumar,Richa Patel,Piyush Ghode,Hardeep Kumar,Anjali Murmu,Nilanchala Sahu,Gayantika Verma,Suresh Kumar Sahu,Sonali Soni,Sujoy Pal,Jagadish Singh,Partha Pratim Roy,Purusottam Banjare
摘要
ABSTRACT The present study aims to find azole‐containing acetylcholinesterase (AChE) inhibitors for the treatment of Alzheimer's disease (AD) through a mixed in silico approach. The first step involved the collection of azole derivatives and predictive quantitative structure–activity relationship (QSAR) model development for their AChE inhibition activity, using multiple linear regressions (MLRs) with the genetic algorithm (GA) for feature selection. The developed GA‐MLR models were statistically robust enough internally ( R 2 a dj = 0.643–0.640, Q 2 LOO = 0.616–0.621) as well as externally ( R 2 pred = 0.626–0.658, R 2 M = 0.562–0.601). The prediction reliability of the models was assured through the leverage approach of the applicability domain. The most significant models were applied to azole‐containing PubChem database compounds, which were classified as active and inactive based on theoretical predictions. The toxicity analysis was also performed for the active compounds by the online web server Protox‐II. The less or nontoxic compounds were subjected to molecular docking, along with donepezil as a standard. Docking analysis revealed that the four compounds have better binding affinity (binding energy = −11.6 to −11.2 kcal/mol) as compared to donepezil (binding energy = −11 kcal/mol). Apart from binding energy, donepezil was observed to be toxic by the prediction from the Protox‐II. Finally, molecular dynamics (MD) analysis of two compounds (Compound 5, having the lowest IC 50 , and Compound 25, having the highest IC 50 among the top 4 docked compounds) not only differentiated them based on final interactions but also exhibited that the toxicity of donepezil might be due to hydrogen bonding with the active site.
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