Hasan Mahmudul, Hossain Md Ifteker, Siddiquee Noimul Hasan, Ahmed Ezaz, Talukder Md Walid Hossain, Rahamatolla Md, Nahar Tasrin, Paul Popy Rani, Suhag Mahmudul Hassan, Uzzaman Monir
Faculty of Science, Department of Microbiology, Noakhali Science and Technology University, Noakhali, Bangladesh.
Drug Design Division, Computer in Chemistry and Medicine Laboratory, Dhaka, Bangladesh.
PLoS One. 2025 Jun 24;20(6):e0326655. doi: 10.1371/journal.pone.0326655. eCollection 2025.
Proton pump inhibitors are essential for treating moderate-to-severe gastroesophageal reflux, peptic ulcers, esophagitis, and related conditions by increasing gastric pH and inhibiting hydrogen ion discharge into the stomach. However, prolonged use may lead to adverse effects along with reduced efficacy. Our research investigates the strategic modification of omeprazole (OMP) derivatives to improve their binding affinity to targeted proteins, thereby enhancing their chemical reactivity, stability, and toxicity profiles. A total of 22 novel OMP analogues were designed through structural alterations, focusing on the benzimidazole and pyridine rings. The geometrical attributes of the analogues were further confirmed through spectral and quantum computational analysis based on density functional theory (DFT) and a B3LYP/6-31G+ G (d, p) basis set. The molecular docking with PTAAC1 presented that most of the analogues had similar or higher binding affinities and nonbonding interactions, including OMP3, OMP19, and OMP21, with binding energies of -7.3, -8.3, and -8.1 kcal/mol compared to the OMP at -7.1 kcal/mol. Pharmacokinetic, biological, and toxicological profiles via ADMET and PASS predictions also demonstrated increased safety and therapeutic potential. MD simulation also showed good stability of OMP3, OMP19, and OMP21 in binding to PTAAC1, and the RMSD, RMSF, ligand RMSD, rGyr, SASA, MolSA, PolSA, and hydrogen bond analysis also suggested superior drug potential compared to OMP. Additionally, the post-simulation MM/GBSA analysis revealed that OMP3 (-36.91 kcal/mol) outperformed OMP19 (-26.45) and OMP21 (-12.61). The protein binding site's high stability and elevated negative binding free energy value further indicate a robust compound-protein interaction with OMP3. However, principal component analysis (PCA) showed the highest variance for OMP21, accounting for 50.66%, 21.58%, and 6.51%, respectively, for PC1, PC2, and PC3. These findings could lead to the development of OMP3 and OMP21 as potential next-generation PPIs with enhanced pharmacological activity and improved side-effect profiles, necessitating more in vitro and in vivo testing.
质子泵抑制剂对于治疗中重度胃食管反流、消化性溃疡、食管炎及相关病症至关重要,其作用机制是提高胃内pH值并抑制氢离子向胃内释放。然而,长期使用可能会导致不良反应,同时疗效降低。我们的研究旨在对奥美拉唑(OMP)衍生物进行策略性修饰,以提高其与靶向蛋白的结合亲和力,从而增强其化学反应性、稳定性和毒性特征。通过结构改变设计了总共22种新型OMP类似物,重点关注苯并咪唑环和吡啶环。基于密度泛函理论(DFT)和B3LYP/6 - 31G+G(d,p)基组,通过光谱和量子计算分析进一步确认了类似物的几何属性。与PTAAC1的分子对接结果表明,大多数类似物具有相似或更高的结合亲和力和非键相互作用,包括OMP3、OMP19和OMP21,其结合能分别为-7.3、-8.3和-8.1 kcal/mol,而OMP的结合能为-7.1 kcal/mol。通过ADMET和PASS预测得到的药代动力学、生物学和毒理学特征也表明其安全性和治疗潜力有所提高。分子动力学模拟还显示OMP3、OMP19和OMP21与PTAAC1结合时具有良好的稳定性,均方根偏差(RMSD)、均方根波动(RMSF)、配体均方根偏差、回转半径(rGyr)、溶剂可及表面积(SASA)、分子表面积(MolSA)、极性表面积(PolSA)和氢键分析也表明它们与OMP相比具有更好的药物潜力。此外,模拟后的MM/GBSA分析表明,OMP3(-36.91 kcal/mol)优于OMP19(-26.45)和OMP21(-12.61)。蛋白质结合位点的高稳定性和升高的负结合自由能值进一步表明OMP3与蛋白质之间存在强大的化合物-蛋白质相互作用。然而,主成分分析(PCA)显示OMP21的方差最高,PC1、PC2和PC3分别占50.66%、21.58%和6.51%。这些发现可能会促使OMP3和OMP21作为具有增强药理活性和改善副作用特征的潜在下一代质子泵抑制剂的开发,这需要更多的体外和体内试验。