Department of clinical pharmacy, Institute for Research and Medical Consultations (IRMC), Imam Abdulrahman Bin Faisal University, P.O. Box 1982, Dammam 31441, Saudi Arabia.
College of Clinical Pharmacy, Imam Abdulrahman Bin Faisal University, P.O. Box 1982, Dammam 31441, Saudi Arabia.
Int J Biol Macromol. 2021 Nov 1;190:301-318. doi: 10.1016/j.ijbiomac.2021.08.207. Epub 2021 Sep 2.
In this study, we have investigated a series of indole-based compounds for their inhibitory study against pancreatic α-amylase and intestinal α-glucosidase activity. Inhibitors of carbohydrate degrading enzymes appear to have an essential role as antidiabetic drugs. All analogous exhibited good to moderate α-amylase (IC = 3.80 to 47.50 μM), and α-glucosidase inhibitory interactions (IC = 3.10-52.20 μM) in comparison with standard acarbose (IC = 12.28 μM and 11.29 μM). The analogues 4, 11, 12, 15, 14 and 17 had good activity potential both for enzymes inhibitory interactions. Structure activity relationships were deliberated to propose the influence of substituents on the inhibitory potential of analogues. Docking studies revealed the interaction of more potential analogues and enzyme active site. Further, we studied their kinetic study of most active compounds showed that compounds 15, 14, 12, 17 and 11 are competitive for α-amylase and non- competitive for α-glucosidase.
在这项研究中，我们研究了一系列吲哚类化合物对胰腺α-淀粉酶和肠道α-葡萄糖苷酶活性的抑制作用。碳水化合物降解酶抑制剂似乎作为抗糖尿病药物具有重要作用。所有类似物对α-淀粉酶（IC = 3.80 至 47.50 μM）和α-葡萄糖苷酶抑制作用（IC = 3.10-52.20 μM）表现出良好到中等的抑制作用，与标准阿卡波糖（IC = 12.28 μM 和 11.29 μM）相比。类似物 4、11、12、15、14 和 17 对两种酶的抑制作用均具有良好的活性潜力。构效关系研究提出了取代基对类似物抑制潜力的影响。对接研究揭示了更多潜在类似物与酶活性部位的相互作用。此外，我们研究了它们对最活跃化合物的动力学研究，结果表明化合物 15、14、12、17 和 11 对 α-淀粉酶是竞争性的，对 α-葡萄糖苷酶是非竞争性的。
