Das Sanjib, Bagchi Arka, Bera Analava, Biswas Arunima, Roy Analabha, Ganguly Rik, Mondal Amalesh, Chattopadhyay Deepanjan, Mondal Paromita Saha, Mondal Tanushree, Samanta Subhasree, Goswami Achintya Mohan, Saha Tanima
Department of Molecular Biology and Biotechnology, University of Kalyani, Kalyani, West Bengal, 741235, India.
Cell and Molecular Biology Laboratory, Department of Zoology, University of Kalyani, Kalyani, Nadia, West Bengal, 741235, India.
Sci Rep. 2025 Jul 2;15(1):23626. doi: 10.1038/s41598-025-08148-2.
Npr1 is an essential protein in C. albicans, maintains ion homeostasis and nutrient transportation at cell membrane, and regulates the activity of ammonium transporter protein Mep2. Npr1 is one of the nine NPR/HAL family kinases classified under "Other groups" in C. albicans. In this study, we had performed protein homology modeling; structure based virtual screening of drugs, docking study and MD simulation. We employed drug repurposing pipeline from which 15 compounds were short listed. Among the compounds, Indacaterol was selected on the basis of high safety profile, binding affinity score value of - 9.3 kcal/mol, as well as its DFG-motif interaction. The best docked pose of the complex was utilized for MD simulation studies. The RMSD values from initial structure and protein-ligand complex were analyzed for the dynamic stability of drug-bound complex and compared with that of the apo-protein. The comparisons of average RMSF values show fluctuation within acceptable range, also very less change of Rg values occur between the protein and protein-ligand throughout the simulation. Further, the complex maintains on an average two hydrogen bonds throughout the simulation period. The binding stability of Npr1 and Indacaterol complex was also verified through Principal Component Analysis. The result secured from these computational approaches and techniques established that the drug has the potential to be developed as an anti-candida lead targeting candidiasis.
Npr1是白色念珠菌中的一种必需蛋白,维持细胞膜上的离子稳态和营养物质运输,并调节铵转运蛋白Mep2的活性。Npr1是白色念珠菌中归类于“其他组”的九个NPR/HAL家族激酶之一。在本研究中,我们进行了蛋白质同源建模、基于结构的药物虚拟筛选、对接研究和分子动力学模拟。我们采用了药物重新利用流程,从中筛选出了15种化合物。在这些化合物中,茚达特罗因其高安全性、结合亲和力评分为-9.3千卡/摩尔以及其DFG模体相互作用而被选中。复合物的最佳对接构象用于分子动力学模拟研究。分析了初始结构和蛋白质-配体复合物的均方根偏差(RMSD)值,以研究药物结合复合物的动态稳定性,并与无配体蛋白进行比较。平均均方根波动(RMSF)值的比较表明波动在可接受范围内,并且在整个模拟过程中蛋白质与蛋白质-配体之间的回旋半径(Rg)值变化也非常小。此外,在整个模拟期间,复合物平均维持两个氢键。通过主成分分析也验证了Npr1与茚达特罗复合物的结合稳定性。从这些计算方法和技术获得的结果表明,该药物有潜力被开发成为一种针对念珠菌病的抗念珠菌先导药物。