Nontoxic and Naturally Occurring Active Compounds as Potential Inhibitors of Biological Targets in Liriomyza trifolii

• Published in: International journal of molecular sciences 2022-11, Vol.23 (21), p.12791
• Main Authors: Shamkh, Israa M., Al-Majidi, Mohammed, Shntaif, Ahmed Hassen, Deng Kai, Peter Tan, Nh-Pham, Ngoc, Rahman, Ishrat, Hamza, Dalia, Khan, Mohammad Shahbaz, Elsharayidi, Maii S., Salah, Eman T., Haikal, Abdullah, Omoniyi, Modupe Akintomiwa, Abdalrahman, Mahmoud A., Karpinski, Tomasz M.
• Format: Article
• Language: English
• Subjects: Acetylcholinesterase; Actin; Arginine kinase; Binding sites; Chlorogenic acid; Energy; Enzymes; Glucosides; Histones; Hydrogen bonds; inhibitory activity; Insect control; Insecticides; Kaempferol; Kinases; Ligands; Liriomyza trifolii; Molecular docking; Molecular dynamics; Phytochemicals; Protease inhibitors; protein inhibitors; protein-ligand interactions; Proteinase inhibitors; Proteins; Tubulin; yeast extraction
• ISSN: 1422-0067; 1661-6596; 1422-0067
• DOI: 10.3390/ijms232112791

In recent years, novel strategies to control insects have been based on protease inhibitors (PIs). In this regard, molecular docking and molecular dynamics simulations have been extensively used to investigate insect gut proteases and the interactions of PIs for the development of resistance against insects. We, herein, report an in silico study of (disodium 5′-inosinate and petunidin 3-glucoside), (calcium 5′-guanylate and chlorogenic acid), chlorogenic acid alone, (kaempferol-3,7-di-O-glucoside with hyperoside and delphinidin 3-glucoside), and (myricetin 3′-glucoside and hyperoside) as potential inhibitors of acetylcholinesterase receptors, actin, α-tubulin, arginine kinase, and histone receptor III subtypes, respectively. The study demonstrated that the inhibitors are capable of forming stable complexes with the corresponding proteins while also showing great potential for inhibitory activity in the proposed protein-inhibitor combinations.