Mengungkap Potensi Senyawa Bioaktif Air Kelapa (Cocos Nucifera) Sebagai Obat Detoksifikasi Racun Merkuri

Authors

  • Baharudin Juni Hermawan Progam Studi Pendidikan Biologi Universitas Nusantara PGRI Kediri
  • Regina Pingkan Setiadji Progam Studi Pendidikan Biologi Universitas Nusantara PGRI Kediri
  • Aida Rohmatul Hidayah Progam Studi Pendidikan Biologi Universitas Nusantara PGRI Kediri
  • Agus Muji Santoso

DOI:

https://doi.org/10.29407/qxr3b244

Keywords:

bioactive, Cocos nucifera, mercury

Abstract

This study aims to reveal the potential of compounds found in coconut water (Cocos nucifera) as detoxifying agents against mercury toxicity. The method used was a descriptive–explorative study with the collection and identification of chemical compound data from the literature. The types of active compounds present in Cocos nucifera were compiled through literature review. Compound IDs, canonical SMILES, biological activities, and Pa values were analyzed in silico using web servers (PubChem and Way2Drug) with a Pa threshold of > 0.7 to predict potential biological activities.

Based on the literature search, three active chemical compounds were identified in Cocos nucifera: valine, tyrosine, and methionine. Valine showed activity as a superoxide dismutase inhibitor (inhibiting oxidative damage) (0.893), a glutamate uptake inhibitor (inhibiting glutamate absorption) (0.854), and a serine–pyruvate transaminase inhibitor (preventing liver damage caused by mercury exposure) (0.833). Tyrosine exhibited activity as a diiodophenylpyruvate reductase inhibitor (preventing the conversion of mercury into toxic forms) (0.928), an FMO3 substrate (producing antioxidants) (0.824), and a muramoyltetrapeptide carboxypeptidase inhibitor (inhibiting mercury entry into cells) (0.799). Finally, methionine showed activity as a pro-opiomelanocortin converting enzyme inhibitor (preventing nerve damage) (0.738), a CYP2H substrate (regulating xenobiotic substrates) (0.717), and a flavin-containing monooxygenase substrate (involved in xenobiotic metabolism) (0.787).

These three compounds have diverse targets in the human body. The results indicate that all three compounds have high Pa scores and various potential activities, particularly in inhibiting enzymes associated with mercury poisoning. This study is expected to contribute to scientific knowledge and serve as a foundation for further research on the development of local plant-based treatments for mercury detoxification.

References

Baum, E. Z., Crespo-Carbone, S. M., Foleno, B., Peng, S., Hilliard, J. J., Abbanat, D., Goldschmidt, R., & Bush, K. (2005). Identification of a dithiazoline inhibitor of Escherichia coli L,D-carboxypeptidase A. Antimicrobial agents and chemotherapy, 49(11), 4500–4507.

Bozkurt, B., Nair, A. P., Misra, A., Scott, C. Z., Mahar, J. H., & Fedson, S. (2022). Neprilysin Inhibitors in Heart Failure: The Science, Mechanism of Action, Clinical Studies, and Unanswered Questions. JACC. Basic to translational science, 8(1), 88–105.

Cashman, J. R. (1995). Structural and catalytic properties of the mammalian flavin-containing monooxygenase. Chemical research in toxicology, 8(2), 165-181.

Cashman, J. R., Akerman, B. R., Forrest, S. M., & Treacy, E. P. (2000). Population-specific polymorphisms of the human FMO3 gene: significance for detoxication. Drug metabolism and disposition: the biological fate of chemicals, 28(2), 169–173.

Choi, M. R., Kouyoumdzian, N. M., Rukavina Mikusic, N. L., Kravetz, M. C., Rosón, M. I., Rodríguez Fermepin, M., & Fernández, B. E. (2015). Renal dopaminergic system: Pathophysiological implications and clinical perspectives. World journal of nephrology, 4(2), 196–212.

Clark, N. E., & Garman, S. C. (2009). The 1.9 a structure of human alpha-N-acetylgalactosaminidase: The molecular basis of Schindler and Kanzaki diseases. Journal of molecular biology, 393(2), 435–447.

Clausen, T., Huber, R., Messerschmidt, A., Pohlenz, H. D., & Laber, B. (1997). Slow-binding inhibition of Escherichia coli cystathionine beta-lyase by L-aminoethoxyvinylglycine: a kinetic and X-ray study. Biochemistry, 36(41), 12633–12643.

Emu, S. (2022). Pengaruh Penambahan Asam Amino Metionin dengan Dosis yang Berbeda dalam Pakan Terhadap Pertumbuhan Ikan Nila Merah. AquaMarine (Jurnal FPIK UNIDAYAN), 9(2), 8-12.

Guo, W., Tan, H. Y., Li, S., Wang, N., & Feng, Y. (2020). Glutamic-Pyruvic Transaminase 1 Facilitates Alternative Fuels for Hepatocellular Carcinoma Growth-A Small Molecule Inhibitor, Berberine. Cancers, 12(7), 1854.

Hadi, M. C. (2013). Bahaya merkuri di lingkungan kita. Jurnal Skala Husada, 10(2), 175-183.

Kumar, A., Taghi Khani, A., Sanchez Ortiz, A., & Swaminathan, S. (2022). GM-CSF: A Double-Edged Sword in Cancer Immunotherapy. Frontiers in immunology, 13, 901277.

Kumar, R. (2024). Decennary Update on Oxidative‐Rearrangement Involving 1, 2‐Aryl C‐C Migration Around Alkenes: Synthetic and Mechanistic Insights. Chemistry–An Asian Journal, e202400053.

Lima, EBC, Sousa, CNS, Meneses, LN, Ximenes, NC, Júnior, S., Vasconcelos, GS, ... & Vasconcelos, SMM (2015). Cocos nucifera (L.)(Arecaceae): Tinjauan fitokimia dan farmakologis. Jurnal Penelitian Medis dan Biologi Brasil , 48 , 953-964.

Loh YP. The effect of pepstatin A, an inhibitor of the pro-opiomelanocortin (POMC)-converting enzyme, on POMC processing in mouse intermediate pituitary. FEBS Lett. 1988 Sep 26;238(1):142-6.

Mustika, I., Tyastirin, E., & Rachmawati, Y. (2018, October). Comparative Morphology of Sperm in The Rat (Rattus novergicus) Exposed to Cadmium (Cd) and Mercury (Hg) with Green Coconut Water (Cocos nucifera L.) as Antidontum. In International Conference on Sustainable Health Promotion (pp. 30-34).

Mycielska, M. E., Mohr, M. T., Schmidt, K., Drexler, K., Rümmele, P., Haferkamp, S., ... & Geissler, E. K. (2019). Potential use of gluconate in cancer therapy. Frontiers in Oncology, 9, 522.

Oleksiak, M. F., Wu, S., Parker, C., Karchner, S. I., Stegeman, J. J., & Zeldin, D. C. (2000). Identification, functional characterization, and regulation of a new cytochrome P450 subfamily, the CYP2Ns. Journal of Biological Chemistry, 275(4), 2312-2321.

Onishi, J., Meinz, M., Thompson, J., Curotto, J., Dreikorn, S., Rosenbach, M., Douglas, C., Abruzzo, G., Flattery, A., Kong, L., Cabello, A., Vicente, F., Pelaez, F., Diez, M. T., Martin, I., Bills, G., Giacobbe, R., Dombrowski, A., Schwartz, R., Morris, S., … Kurtz, M. B. (2000). Discovery of novel antifungal (1,3)-beta-D-glucan synthase inhibitors. Antimicrobial agents and chemotherapy, 44(2), 368–377.

Perona, J. J. (2013). Glutaminyl-tRNA synthetases. In Madame Curie Bioscience Database [Internet]. Landes Bioscience.

Pithadia, A. B., & Jain, S. M. (2009). 5-Hydroxytryptamine Receptor Subtypes and their Modulators with Therapeutic Potentials. Journal of clinical medicine research, 1(2), 72–80.

Rachmawati, Y., Mustika, I., Tyastirin, E., WATI, R., ARIFA, A., AZZAHRA, H., ... & NINGRUM, I. (2020). Effectiveness of green coconut (Cocos nucifera L.) water against heavy metal levels in the blood of rattus norvegicus. In Proceedings of the Built Environment, Science and Technology International Conference (pp. 113-118).

Santosa, B., Ariyadi, T., Bintanah, S., Fristiani, A. K. B., & Damayanti, F. N. THE COMBINATION OF IR BAGENDIT RICE LEAF WATER EXTRACT AND COCONUT WATER REDUCES OXIDANT ACTIVITY AND IMPROVES THE MORPHOLOGY AND FUNCTION OF KIDNEY CELLS AFTER MERCURY EXPOSURE.

Slaughter, J. C., & Davies, D. D. (1968). Inhibition of 3-phosphoglycerate dehydrogenase by l-serine. The Biochemical journal, 109(5), 749–755.

Sulistia, A., Sulistiarini, R., & Masruhim, M. A. (2016). Aktivitas Antidotum Air Kelapa Hijau (Cocos nucifera L.) terhadap Keracunan Sianida Pada Mencit (Mus musculus L.). Journal of Tropical Pharmacy and Chemistry, 3(3), 191-196.

Surmiak E, Magiera-Mularz K, Musielak B, Muszak D, Kocik-Krol J, Kitel R, Plewka J, Holak TA, Skalniak L. PD-L1 Inhibitors: Different Classes, Activities, and Mechanisms of Action. Int J Mol Sci. 2021

Veith, A., Urich, T., Seyfarth, K., Protze, J., Frazão, C., & Kletzin, A. (2011). Substrate pathways and mechanisms of inhibition in the sulfur oxygenase reductase of acidianus ambivalens. Frontiers in microbiology, 2, 37.

Venugopal, A., & Joseph, D. (2017). Cocos nucifera: It’s pharmacological activities. World Journal of Pharmaceutical Sciences, 195-200.

Whitelaw, B. S., & Robinson, M. B. (2013). Inhibitors of glutamate dehydrogenase block sodium-dependent glutamate uptake in rat brain membranes. Frontiers in endocrinology, 4, 123.

Xu, Y., & Sun, Z. (2017). Regulation of S-formylglutathione hydrolase by the anti-aging gene klotho. Oncotarget, 8(51), 88259–88275.

Younus H. (2018). Therapeutic potentials of superoxide dismutase. International journal of health sciences, 12(3), 88–93.

Downloads

Published

2026-05-08

How to Cite

Mengungkap Potensi Senyawa Bioaktif Air Kelapa (Cocos Nucifera) Sebagai Obat Detoksifikasi Racun Merkuri. (2026). Prosiding Seminar Nasional Hayati, 3(1), 179-184. https://doi.org/10.29407/qxr3b244

Similar Articles

You may also start an advanced similarity search for this article.

Most read articles by the same author(s)

1 2 3 > >>