Main Article Content
Anticoagulants are very important for the treatment and prevention of thrombotic disorders. The use of conventional anticoagulants like heparin and warfarin can cause bleeding complications. To find safer anticoagulant therapy agents, the development of isolation of new anticoagulant compounds has shifted towards natural sources. Bioactive peptides can be considered a better alternative because of their therapeutic potential in the treatment of various diseases. Several peptide molecules have been shown to inhibit the cytochrome P450 (CYP) 2C9 enzyme as a natural anticoagulant, such as bioactive peptides produced by yellowfin sole (Limanda aspera) and bioactive peptides in blue mussel (Mytilus edulis). This study aims to identify and evaluate the interactions that occur between peptide molecules with the cytochrome P450 (CYP) 2C9 enzyme using protein-peptide docking methods. Bioactive peptide sequencing was modeled using the PEP-FOLD software. The best conformation was chosen for an interaction study against the macromolecule of cytochrome P450 (CYP) 2C9 enzyme using PatchDock software. Further observations were made of interactions formed using BIOVIA Discovery Studio 2020 software. Based on the results of protein-peptide docking, the yellowfin sole peptide molecule has a good affinity against the macromolecule of cytochrome P450 (CYP) 2C9 enzyme, with an ACE score of −2527.01 kJ / mol. Therefore, the bioactive peptide is predicted to be used as a candidate for the cytochrome P450 (CYP) 2C9 enzyme inhibitor.
This work is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License.
- Ahmed, I., Majeed, A., & Powell, R. (2007). Heparin induced thrombocytopenia: diagnosis and management update. Postgrad Med J, 83, 575-582. https://doi.org/10.1136/pgmj.2007.059188
- Akif, M., Masuyer, G., Schwager, S.L.U., Bhuyan, B.J., Mugesh, G., Isaac, R.E., Sturrock, E.D., & Acharya, K.R. (2011). Structural characterization of angiotensin I-converting enzyme in complex with a selenium analogue of captopril. FEBS J, 2011, 278, 3644-3650. http://doi.org/10.1111/j.1742-4658.2011.08276.x
- Alquwaizani, M., Buckley, L., Adams, C., & Fanikos, J. (2013). Anticoagulants: a review of the pharmacology, dosing, and complications. Curr Emerg Hosp Med Rep, 1, 83-97. https://doi.org/10.1007/s40138-013-0014-6
- Aruleba, R.T., Adekiya, T.A., Oyinloye, B.E., & Kappo, A.P. (2018). Structural studies of predicted ligand binding sites and molecular docking analysis of Slc2a4 as a therapeutic target for the treatment of cancer. Int J Mol Sci, 19. https://doi.org/10.3390/ijms19020386
- Chavan, S.G., & Deobagkar, D.D. (2015). An in silico insight into novel therapeutic interaction of LTNF Peptide-LT10 and design of structure based peptidomimetics for putative anti-diabetic activity. PLoS One, 10, e0121860. https://doi.org/10.1371/journal.pone.0121860
- Franchini, M., & Mannucci, P.M. (2016). Direct oral anticoagulants and venous thromboembolism. Eur Respir Rev, 25, 295-302. https://doi.org/10.1183/16000617.0025-2016
- Harter, K., Levine, M., & Henderson, S.O. (2015). Anticoagulation drug therapy: a review. West J Emerg Med, 16, 11-17. https://doi.org/10.5811/westjem.2014.12.22933
- Hawkins, D. (2004). Limitations of traditional anticoagulants. Pharmacother, 24, 62-65. https://doi.org/10.1592/phco.24.10.62s.36120
- Jung, W.K., & Kim S.K. (2009). Isolation and characterisation of an anticoagulant oligopeptide from blue mussel, Mytilus edulis. Food Chem, 117, 687-692. https://doi.org/10.1016/j.foodchem.2009.04.077
- Katritsis, D.G., Gersh, B.J., & Camm, A.J. (2015). Anticoagulation in atrial fibrillation current concepts. Arrhythm Electrophysiol Rev, 4, 100–107. https://doi.org/10.15420/aer.2015.04.02.100
- Kemmish, H., Fasnacht, M., & Yan, L. (2017). Fully automated antibody structure prediction using BIOVIA tools: Validation study. PLoS One, 12, e0177923. https://doi.org/10.1371/journal.pone.0177923
- Kurniawan, F., Miura, Y., Kartasasmita, R.E., Yoshioka, N., Mutalib, A., & Tjahjono, D.H. (2018). In silico study, synthesis, and cytotoxic activities of porphyrin derivatives. Pharmaceuticals, 11, 8. https://doi.org/10.3390/ph11010008
- Mackman, N. (2012). New insights into the mechanisms of venous thrombosis. J Clin Investig, 122, 2331-2336. https://doi.org/10.1172/JCI60229.paralysis
- Mega, J.L., & Simon, T. (2015). Novel antithrombotic agents 1 pharmacology of antithrombotic drugs: an assessment of oral antiplatelet and anticoagulant treatments. Lancet, 386, 281-291. https://doi.org/10.1016/S0140-6736(15)60243-4
- Norel, R., Sheinerman, F., Petrey, D., & Honig, B. (2001). Electrostatic contributions to protein–protein interactions: Fast energetic filters for docking and their physical basis. Protein Sci, 10, 2147-2161. https://doi.org/10.22159/10.1110/ps.12901
- Patterson, S.L., LaMonte, M.P., Mikdashi, J.A., Haines, S.T., & Hursting, M.J. (2006). Anticoagulation strategies for treatment of ischemic stroke and antiphospholipid syndrome: case report and review of the literature. Pharmacotherapy, 26, 1518-1525. https://doi.org/10.1592/phco.26.10.1518
- Prabhu, D.S., & Rajeswari, V.D. (2016). In silico docking analysis of bioactive compounds from Chinese medicine Jinqi Jiangtang Tablet (JQJTT) using Patch Dock. J Chem Pharm Res, 8, 15-21.
- Rajapakse, N., Jung, W.K., Mendis, E., Moon, S.H., & Kim, S.K. (2005). A novel anticoagulant purified from fish protein hydrolysate inhibits factor XIIa and platelet aggregation. Life Sci,
- 76, 2607-2619. https://doi.org/10.1016/j.lfs.2004.12.010
- Raskob, G.E., Angchaisuksiri, P., Bianco, A.N., Buller, H., Gallus, A., Hunt, B.J., Hylek, E.M., Kakkar, A., Konstantinides, S.V., McCumber, M., Ozaki, Y., Wendelboe, A., & Weitz, J.I. (2014). Thrombosis: a major contributor to the global disease burden. J Thromb Haemost, 12, 1580-1590. https://doi.org/10.1111/jth.12698
- Shen, Y., Maupetit, J., Derreumaux, P., & Tuffery, P. (2014). Improved PEP-FOLD approach for peptide and miniprotein structure prediction. J Chem Theory Comput, 10, 4745-4758. https://doi.org/10.1021/ct500592m
- Snipelisky, D., & Kusumoto, F. (2013). Current strategies to minimize the bleeding risk of warfarin. J Blood Med, 4, 89-99. https://doi.org/10.2147/JBM.S41404
- Suguna, S., Kunkulol, R., Kumar, V., Ambadasu, B., & Nandal, D.H. (2014). Affinity of warfarin with cyp2c9 by molecular docking study. Int J Pharm Pharm Sci. 6, 181-182.
- Thevenet, P., Shen, Y., Maupetit, J., Guyon, F., Derreumaux, P., & Tuffery, P. (2012). PEP-FOLD: an updated de novo structure prediction server for both linear and disulfide bonded cyclic peptides. Nucleic Acids Res, 2012, 40, 288-293. https://doi.org/10.1093/nar/gks419
- Veeraragavan, V., Narayanaswamy, R., & Chidambaram, R. (2017). Predicting the biodegradability nature of imidazole and its derivatives by modulating two histidine degradation enzymes (urocanase and formiminoglutamase) activities. Asian J Pharm Clin Res, 10, 383-386. https://doi.org/10.22159/ajpcr.2017.v10i11.20999
- Wang, X., Yu, H., Xing, R., & Li, P. (2017). Characterization, preparation, and purification of marine bioactive peptides. Biomed Res Int, 9746720. https://doi.org/10.1155/2017/9746720