Dergiler / Hacettepe Journal of Biology and Chemistry / 2026 / Volume: 53 Issue: 4

Analyses and Comparisons of the Antimicrobial-Cytotoxic Effects and Molecular Docking Study of L-DOPA and L-DOPA Methyl Ester

Tuğçe Deniz Karaca(GAZİ ÜNİVERSİTESİ, SAĞLIK HİZMETLERİ MESLEK YÜKSEKOKULU)0000-0002-7471-1759
Hüseyin Balcı(GEBZE TECHNICAL UNIVERSITY)0000-0002-8778-4586
Arzu Aysan(GEBZE TECHNICAL UNIVERSITY)0000-0001-7217-3347
Yusuf Sert(BOZOK ÜNİVERSİTESİ)0000-0001-8836-8667
Sayfa
—
Yayın Tarihi
2025-10-01
🏛️Bu makalenin bibliyografik verileri ve tam metin bağlantısı DergiPark üzerinden sağlanmıştır.
DergiPark Kaydı ↗
✨

Yapay Zeka Hızlı Bakış & Çıkarımlar

AI Insight
⚡ TL;DR(1 Cümlede Hızlı Çıkarım)

The results obtained are new and it is thought that these results of the study will contribute to the development of new synthesizable drug studies.

📌 3 Maddede Bu Makale

🎯
Amaç & Hipotez:The increasing the importance of synthesizing compounds with high biocompatibility, low cytotoxicity, and advanced antibacterial properties is evident in current research.
📊
Temel Bulgular & Veri:L-3,4-Dihydroxyphenylalanine (L-DOPA) is a crucial drug widely used in the treatment of Parkinson's disease.
💡
Sonuç & Katkı:The results obtained are new and it is thought that these results of the study will contribute to the development of new synthesizable drug studies.
🔬Tür:Research Article
📍Kapsam:Genişletilmiş Akademik Örneklem
⚙️Değişkenler:L-Dopa-ester · Antimicrobial activity · Cytotoxicity

Abstract

The increasing the importance of synthesizing compounds with high biocompatibility, low cytotoxicity, and advanced antibacterial properties is evident in current research. L-3,4-Dihydroxyphenylalanine (L-DOPA) is a crucial drug widely used in the treatment of Parkinson's disease. In this study, we investigated the antimicrobial and cytotoxic effects of L-DOPA and its water-soluble derivative, L-DOPA methyl ester. The antimicrobial effects of L-DOPA and L-DOPA Methyl Ester were tested on both Gram-negative and Gram-positive bacteria. Additionally, the impact of L-DOPA and its ester on cell viability was assessed using the MTT assay on cancerous and non-cancerous cell lines. The study revealed that both substances were effective against Gram-positive bacteria but not Gram-negative bacteria. Specifically, the growth of Gram-positive bacteria was inhibited by both compounds, with L-DOPA showing greater efficacy. We also observed that L-DOPA and its ester exhibit anti-cancer activity. Furthermore, the molecular docking mechanism between the three targets (2DS2, 4URO and 1M17) and the compounds was investigated using Autodock Vina. The findings show that the L-DOPA molecule is more appropriately attached to the target receptors than the L-DOPA methyl ester molecule. As a result, its inhibition is greater. The results obtained are new and it is thought that these results of the study will contribute to the development of new synthesizable drug studies.

🔖

Bu Makaleye Atıf Yap

Karaca, T. D., Balcı, H., Aysan, A., Sert, Y. (2025). Analyses and Comparisons of the Antimicrobial-Cytotoxic Effects and Molecular Docking Study of L-DOPA and L-DOPA Methyl Ester. Hacettepe Journal of Biology and Chemistry, Volume: 53 Issue: 4. https://doi.org/10.15671/hjbc.1684535

📄 Tam Metin PDF Okuyucu

📄

PDF görüntüleyici hazırlanıyor...

Kaynakça (39)

  1. S.T. Cole, Who will develop new antibacterial agents? Philos. Trans. R. Soc. Lond. B. Biol. Sci., 369 (1645) (2014) 20130430.
  2. A. Pinazo, R. Pons, L. Perez, M.R. Infante, Amino acids as raw material for biocompatible surfactants, Ind. Eng. Chem. Res., 50 (9) (2011) 4805–4817.
  3. M. Markovic, S. Ben-Shabat, A. Dahan Prodrugs for Improved Drug Delivery: Lessons Learned from Recently Developed and Marketed Products Pharmaceutics, 12 (11) (2020) 1031-1043.
  4. X. Sun, S.Vilar, N.P. Tatonetti, High-throughput methods for combinatorial drug discovery. Sci. Transl. Med., 5 (2013) 201-205.
  5. D. Gupta, D. Bhatia, V. Dave, V. Sutariya, Varghese Gupta, S., Salts of Therapeutic Agents: Chemical, Physicochemical, and Biological Considerations, Molecules, 23 (2018) 1719.
  6. V.J.Stella, K.W. Nti-Addae, Prodrug strategies to overcome poor water solubility, Adv. Drug Deliv. Rev., 59 (2007) 677–694.
  7. Y. T. H. Lam, M.G. Ricardo, R.Rennert, A. Frolov, A.Porzel, W. Brandt, P. Stark, B. Westermann, N. Arnold, Rare glutamic acid methyl ester peptaibols from Sepedonium ampullosporum damon KSH 534 exhibit promising antifungal and anticancer activity. Int. J. Mo.l Sci., 22 (23) (2021) 12718.
  8. N. Joondan, S. Jhaumeer-Laulloo, P. Caumul, A study of the antibacterial activity of L-phenylalanine and L-tyrosine esters in relation to their CMC and their interactions with 1,2-dipalmitoylsn- glycero-3-phosphocholine, DPPC as model membrane. Microbiol. Res., 169 (2014) 675–685.
  9. N. Joondan, P. Caumul, M. Akerman, S. Jhaumeer-Laulloo, Synthesis, micellization and interaction of novel quaternary ammonium compounds derived from L-phenylalanine with 1,2-dipalmitoyl-sn-glycero-3-phosphocholine as model membrane in relation to their antibacterial activity, and their selectivity over human red blood cells, Bioorg. Chem., 58 (2015) 117–129.
  10. A. Bratuša, T. Elschner, T. Heinze, E. Fröhlich, S.Hribernik, M.Božič, E. Žagar, K.S. Kleinschek, M.Thonhofer, R. Kargl, Functional dextran amino acid ester particles derived from N-protected S-trityl-L-cysteine, Colloids Surf. B., 1:181 (2019) 561-566.
  11. J.A.S. Almeida, M.C. Moran, M.R. Infante, A.A.C.C. Pais, Interaction of arginine-based cationic surfactants with lipid membrane. An experimental and molecular simulation study, Arkivoc, 34 (2010) 34–40.
  12. N. Lozano, L. Perez, R. Pons, J.R. Luque-Ortega, M. Fernandez-Reyes, L. Rivas, A. Pinazo, Interaction studies of diacyl glycerol arginine-based surfactants with DPPC and DMPC monolayers, relation with antimicrobial activity, Colloids Surf. A., 319 (2008) 196-203.
  13. S. Fahn MD, Levodopa in the treatment of Parkinson’s disease, Oxidative Stress and Neuroprotection J. Neural Transm. Suppl., 71 (2006) 1-15.
  14. R. Hernández-Altamirano, V. Y. Mena-Cervantes, T.E. Chávez-Miyauchi, D.A. Nieto-Álvarez, M. A. Domínguez-Aguilar, L. S. Zamudio-Rivera,V. Barba, F.J. Fernández-Perrino, S. Pérez-Miranda f, H. I. Beltrán, New bis-di-organotin compounds derived from aminoacid-imine-hexadentate ligands, Multifunctional evaluation as corrosion inhibitors, antibacterials and asphaltene dispersants/inhibitors, Polyhedron, 52 (22) (2013) 301-307.
  15. D.R. Cooper, C.Marrel, B. Testa, H. Van de Waterbeemd, N. Quinn, P. Jenner, C.D., Marsden, L-Dopa methyl ester--a candidate for chronic systemic delivery of L-Dopa in Parkinson's disease, Clin. Neuropharmacol., 7(1) (1984) 89-98.
  16. D.R.Cooper, C. Marrel, H. Van de Waterbeemd, B. Testa, P.Jenner, C.D.Marsden, L-dopa esters as potential prodrugs: effect on brain concentration of dopamine metabolites in reserpinized mice, J. Pharm. Pharmacol., 39 (10) (1987) 809-18.
  17. N.Furukawa, Y. Goshima, T. Miyamae, Y.Sugiyama, M. Shimizu, E. Ohshima, F. Suzuki, N. Arai, K. Fujita, Y. Misu, L-DOPA Cyclohexyl ester is a novel potent and relatively stable competitive antagonist against L-DOPA among several L-DOPA ester compounds, Jpn. J. Pharmacol., 82 (2000) 40-47.
  18. N. Joondan, S. Jhaumeer-Laulloo, P. Caumul, Effect of Chain Length on the micellization, antibacterial, DPPC interaction and antioxidant activities of L-3,4- Dihydroxyphenylalanine (L-DOPA) esters, J. Surfact. Deterg., (2015) 18:1095–1104.
  19. M.M. Wick, L-Dopa methyl ester as a new antitumour agent, Nat., 269 (1977).
  20. M. Balouiri, M. Sadiki, S.K. Ibnsouda, Methods for in vitro evaluating antimicrobial activity: A review, J. Pharm. Anal., 6 (2) (2016) 71-79.
  21. O. Yermolaieva, R. Xu, C. Schinstock, N. Brot, H. WEissbach, S.H. Heinemann, T. Hoshi, Methionine sulfoxide reductase A protects neuronal cells against brief hypoxia/reoxygenation, Proc. Natl. Acad. Sci. U.S.A., 101 (5) (2004) 1159-1164.
  22. M.J. Frisch, G. Trucks, H. Schlegel, G. Scuseria, M. Robb, J. Cheeseman, G. Scalmani, V. Barone, B. Mennucci, G. Petersson, Gaussian 09, Revision D. 01, Gaussian, Inc. Wallingford, CT (2009).
  23. R. Dennington, T. Keith, J. Millam, GaussView, version 5, Semichem Inc.: Shawnee Mission, KS (2009).
  24. O. Trott, A.J. Olson, AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading, J. Comput. Chem., 31 (2) (2010) 455-461.
  25. A.Thakur, S. Ranote, D. Kumar, K.K. Bhardwaj, R. Gubta, G.S. Chauhan, Synthesis of a PEGylated dopamine ester with enhanced antibacterial and antifungal activity, ACS Omega, 3 (7) (2018) 7925-7933.
  26. T.J. Silhavy, D. Kahne, S. Walker, The Bacterial Cell Envelope, Cold Spring Harb. Perspect. Biol., 2 (5) (2010) 000414.
  27. N. Malanovic, K. Lohner, Gram-positive bacterial cell envelopes: The impact on the activity of antimicrobial peptides, Biochim. Biophys. Acta- Biomembr., 1858 (5) (2016) 936-946.
  28. M. Sushomasri, S.M. Himangshu, C. Pranabesh, G.D. Sujata, Potential of dopamine hydrochloride as a novel antimicrobial agent, Int. J. Biomed. Pharm. Sci., 4 (2 ) (2010) 70-75.
  29. J. Lellouche, E. Kahana, S. Elias, A. Gedanken, E.Banin, Antibiofilm activity of nanosized magnesium flüoride, J. Biomater., 30 (2009) 5969-5978.
  30. S.H.Kaufmann, S. Desnoyers, Y. Ottaviano, N.E. Davidson, G.G.Poirier, Specific Proteolytic Cleavage of Poly(ADP-ribose) Polymerase: An Early Marker of Chemotherapy-induced Apoptosis, Cancer Research, 53 (1993) 3976–3985.
  31. M.Tewari, L.T. Quan, K. O’Rourke, S. Desnoyers, Z. Zeng, D.R. Beidler, G.G. Poirier, G.S. Salvesen, V.M. Dixit, Yama/ CPP32b, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly (ADP-ribose) polymerase, Cell, 81 (1995) 801–809.
  32. Y. Zhang, A. Dimtchev, A. Dritschilo, M. Jung, Ionizing Radiation-induced Apoptosis in Ataxia-Telangiectasia Fibroblasts: Roles of caspase-9 and cellular inhibitor of apoptosis protein-1, J. Biol. Chem., 276 (2001) 28842–28848.
  33. B.J. McConkey, V. Sobolev, M. Edelman, The performance of current methods in ligand–protein docking, Curr. Sci., 83 (7) (2002) 845-856.
  34. S.F. Sousa, P.A. Fernandes, M.J. Ramos, Protein–ligand docking: current status and future challenges, Proteins: Struct., Funct., Bioinf., 65 (1) (2006) 15-26.
  35. D.-F. Li, P. Jiang, D.-Y. Zhu, Y. Hu, M. Max, D.-C. Wang, Crystal structure of II: a structural type of sweet proteins and the main structural basis for its sweetness, J. Struct. Biol., 162 (1) (2008) 50-62.
  36. J. Lu, S. Patel, N. Sharma, S.M. Soisson, R. Kishii, M. Takei, Y. Fukuda, K.J. Lumb, S.B. Singh, Structures of kibdelomycin bound to Staphylococcus aureus GyrB and ParE showed a novel U-shaped binding mode, ACS Chem. Biol., 9 (9) (2014) 2023-2031.
  37. J. Stamos, M.X. Sliwkowski, C. Eigenbrot, Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor, J. Biol. Chem., 277 (48) (2002) 46265-46272.
  38. S.F Sousa, P.A Fernandes, M.J Ramos, Protein–ligand docking: current status and future challenges, Proteins: Struct., Funct., Bioinf., 65 (1) (2006) 15-26.
  39. T.Kimmerlin, Discovery and optimization of isoquinoline ethyl ureas as antibacterial agents, J. Med. Chem., 60 (9) (2017) 3755-3775.