Alhakamy Nabil Abdulhafiz, Mohamed Gamal Abdallah, Fahmy Usama Ahmed, Eid Basma Ghazi, Ahmed Osama Abdelhakim Aly, Al-Rabia Mohammed Wanees, Khedr Amgad Ibrahim Mansour, Nasrullah Mohammed Zahid, Ibrahim Sabrin Ragab Mohamed
Department of Pharmaceutics, Faculty of Pharmacy, King Abdulaziz University, Jeddah 21589, Saudi Arabia.
Center of Excellence for Drug Research and Pharmaceutical Industries, King Abdulaziz University, Jeddah 21589, Saudi Arabia.
Life (Basel). 2022 Mar 7;12(3):384. doi: 10.3390/life12030384.
Two new benzophenones: garcimangophenones A () and B () and five formerly reported metabolites were purified from the pericarps EtOAc fraction of ((GM) Clusiaceae). Their structures were characterized by various spectral techniques and by comparing with the literature. The α-amylase inhibitory (AAI) potential of the isolated metabolites was assessed. Compounds and had significant AAI activity (IC 9.3 and 12.2 µM, respectively) compared with acarbose (IC 6.4 µM, reference α-amylase inhibitor). On the other hand, had a moderate activity. Additionally, their activity towards the α-amylase was assessed utilizing docking studies and molecular dynamics (MD) simulations. The docking and predictive binding energy estimations were accomplished using reported crystal structure of the α-amylase (PDB ID: 5TD4). Compounds and possessed highly negative docking scores of -11.3 and -8.2 kcal/mol, when complexed with 5TD4, respectively while acarbose had a docking score of -16.1 kcal/mol, when complexed with 5TD4. By using molecular dynamics simulations, the compounds stability in the complexes with the α-amylase was analyzed, and it was found to be stable over the course of 50 ns. The results suggested that the benzophenone derivative may be potential α-amylase inhibitors. However, further investigations to support these findings are required.
从藤黄科植物藤黄（GM）的果皮乙酸乙酯提取物中分离得到两种新的二苯甲酮：藤黄二苯甲酮A（）和B（）以及五种之前报道过的代谢产物。通过各种光谱技术并与文献对比对它们的结构进行了表征。评估了分离得到的代谢产物的α-淀粉酶抑制（AAI）潜力。与阿卡波糖（IC50为6.4μM，α-淀粉酶抑制剂对照品）相比，化合物和具有显著的AAI活性（IC50分别为9.3和12.2μM）。另一方面，具有中等活性。此外，利用对接研究和分子动力学（MD）模拟评估了它们对α-淀粉酶的活性。对接和预测结合能估计是使用已报道的α-淀粉酶晶体结构（PDB ID：5TD4）完成的。化合物和与5TD4复合时，对接分数分别为-11.3和-8.2 kcal/mol，呈高度负值，而阿卡波糖与5TD4复合时对接分数为-16.1 kcal/mol。通过分子动力学模拟，分析了化合物与α-淀粉酶形成的复合物的稳定性，发现其在50 ns过程中是稳定的。结果表明二苯甲酮衍生物可能是潜在的α-淀粉酶抑制剂。然而，需要进一步研究来支持这些发现。
