Kumar Harish B, Manandhar Suman, Rathi Ekta, Kabekkodu Shama Prasada, Mehta Chetan Hasmukh, Nayak Usha Yogendra, Kini Suvarna G, Pai K Sreedhara Ranganath
Department of Pharmacology, Manipal College of Pharmaceutical Sciences, Manipal Academy of Higher Education, Manipal, Karnataka, 576104, India.
Department of Pharmaceutical Chemistry, Manipal College of Pharmaceutical Sciences, Manipal Academy of Higher Education, Manipal, Karnataka, 576104, India.
Mol Divers. 2024 Jun;28(3):1485-1503. doi: 10.1007/s11030-023-10671-1. Epub 2023 Jul 3.
The Akt pathway plays a significant role in various diseases like Alzheimer's, Parkinson's, and Diabetes. Akt is the central protein whose phosphorylation controls many downstream pathways. Binding of small molecules to the PH domain of Akt facilitates its phosphorylation in the cytoplasm and upregulates the Akt pathway. In the current study, to identify Akt activators, ligand-based approaches like 2D QSAR, shape, and pharmacophore-based screening were used, followed by structure-based approaches such as docking, MM-GBSA, ADME prediction, and MD simulation. The top twenty-five molecules from the Asinex gold platinum database found to be active in most 2D QSAR models were used for shape and pharmacophore-based screening. Later docking was performed using the PH domain of Akt1 (PDB: 1UNQ), and 197105, 261126, 253878, 256085, and 123435 were selected based on docking score and interaction with key residues, which were druggable and formed a stable protein-ligand complex. MD simulations of 261126 and 123435 showed better stability and interactions with key residues. To further investigate the SAR of 261126 and 123435, derivatives were downloaded from PubChem, and structure-based approaches were employed. MD simulation of derivatives 12289533, 12785801, 83824832, 102479045, and 6972939 was performed, in which 83824832 and 12289533 showed interaction with key residues for a longer duration of time, proving that they may act as Akt activators.
Akt信号通路在阿尔茨海默病、帕金森病和糖尿病等多种疾病中发挥着重要作用。Akt是核心蛋白,其磷酸化控制着许多下游通路。小分子与Akt的PH结构域结合可促进其在细胞质中的磷酸化,并上调Akt信号通路。在本研究中,为了鉴定Akt激活剂,使用了基于配体的方法,如二维定量构效关系(2D QSAR)、形状和药效团筛选,随后采用了基于结构的方法,如对接、MM-GBSA、药物代谢动力学(ADME)预测和分子动力学(MD)模拟。从Asinex金铂数据库中筛选出在大多数二维定量构效关系模型中具有活性的前25个分子,用于形状和药效团筛选。随后,使用Akt1的PH结构域(PDB:1UNQ)进行对接,并根据对接分数和与关键残基的相互作用选择了197105、261126、253878、256085和123435,这些残基是可成药的,并形成了稳定的蛋白质-配体复合物。对261126和123435进行的分子动力学模拟显示出更好的稳定性以及与关键残基的相互作用。为了进一步研究261126和123435的构效关系,从PubChem下载了衍生物,并采用了基于结构的方法。对衍生物12289533、12785801、83824832、102479045和6972939进行了分子动力学模拟,其中83824832和12289533与关键残基的相互作用持续时间更长,证明它们可能作为Akt激活剂发挥作用。