Antibacterial Potency of Bioactive Compounds from Areca catechu Nuts: A Molecular Docking Study Targeting 8H1B
Abstract
Areca catechu, a plant in the Arecaceae family, is rich in bioactive secondary metabolite compounds. Areca catechu has many benefits and potentials, including its antibacterial properties. This study aims to describe the potential of secondary metabolite compounds as antibacterials targeted at 8H1B and their toxicity profile through in silico analysis. The ligands used in this study were catechin, acatechu B, jacareubin, clindamycin as a comparison compound, and S-adenosylmethionine as a native ligand. The results showed that acatechu B had the lowest binding energy (-12.66 kcal/mol) compared to catechin (-9.44 kcal/mol), jacareubin (-8.99 kcal/mol), clindamycin (-10.93 kcal/mol), and S-adenosylmethionine (-11.76 kcal/mol). According to Biovia Discovery simulations, the Areca catechu bioactive compound interacts with 8H1B through van der Waals, conventional hydrogen bonds, and different variants of pi interaction. The toxicity profiles of the Areca catechu bioactive compound showed that they were not hepatotoxic, not mutagenic, not carcinogenic, and had safe LD50 values. These results suggest that the Areca catechu bioactive compound possesses antibacterial potential by targeting 8H1B.
Keywords
References
S. Gunjal et al., “An Overview on Betel Quid and Areca Nut Practice and Control in Selected Asian and South East Asian Countries,” Substance Use and Misuse, vol. 55, no. 9. Taylor and Francis Ltd, pp. 1533–1544, Jun. 01, 2020. doi: 10.1080/10826084.2019.1657149.
M. Rashid, S. Shamsi, R. Zaman, and A. Ilahi, “ARECA CATECHU: ENFOLDING OF HISTORICAL AND THERAPEUTIC TRADITIONAL KNOWLEDGE WITH MODERN UPDATE,” International Journal of Pharmacognosy, vol. 2, no. 5, pp. 221–228, 2015, doi: 10.13040/IJPSR.0975-8232.IJP.2(5).221-28.
H. Sun, W. Yu, H. Li, X. Hu, and X. Wang, “Bioactive Components of Areca Nut: An Overview of Their Positive Impacts Targeting Different Organs,” Nutrients, vol. 16, no. 5. Multidisciplinary Digital Publishing Institute (MDPI), Mar. 01, 2024. doi: 10.3390/nu16050695.
A. Ansari et al., “Areca catechu: A phytopharmacological legwork,” Food Frontiers, vol. 2, no. 2. John Wiley and Sons Inc, pp. 163–183, Jun. 01, 2021. doi: 10.1002/fft2.70.
M. N. de Canha, S. Komarnytsky, L. Langhansova, and N. Lall, “Exploring the Anti-Acne Potential of Impepho [Helichrysum odoratissimum (L.) Sweet] to Combat Cutibacterium acnes Virulence,” Front Pharmacol, vol. 10, 2020, doi: 10.3389/fphar.2019.01559.
L. W. Chen, H. L. Chung, C. C. Wang, J. H. Su, Y. J. Chen, and C. J. Lee, “Anti-acne effects of cembrene diterpenoids from the cultured soft coral sinularia flexibilis,” Mar Drugs, vol. 18, no. 10, Oct. 2020, doi: 10.3390/md18100487.
M. Fournière, T. Latire, D. Souak, M. G. J. Feuilloley, and G. Bedoux, “Staphylococcus epidermidis and cutibacterium acnes: Two major sentinels of skin microbiota and the influence of cosmetics,” Microorganisms, vol. 8, no. 11. MDPI AG, pp. 1–31, Nov. 01, 2020. doi: 10.3390/microorganisms8111752.
R. Gamble et al., “Topical Antimicrobial Treatment of Acne Vulgaris An Evidence-Based Review,” 2012.
M. Kanlayavattanakul and N. Lourith, “Therapeutic agents and herbs in topical application for acne treatment,” International Journal of Cosmetic Science, vol. 33, no. 4. pp. 289–297, Aug. 2011. doi: 10.1111/j.1468-2494.2011.00647.x.
I. Kurokawa et al., “New developments in our understanding of acne pathogenesis and treatment,” Experimental Dermatology, vol. 18, no. 10. pp. 821–832, Oct. 2009. doi: 10.1111/j.1600-0625.2009.00890.x.
A. G. Torres, E. Batlle, and L. Ribas de Pouplana, “Role of tRNA modifications in human diseases,” Trends in Molecular Medicine, vol. 20, no. 6. Elsevier Ltd, pp. 306–314, 2014. doi: 10.1016/j.molmed.2014.01.008.
S. Goto-Ito, T. Ito, M. Kuratani, Y. Bessho, and S. Yokoyama, “Tertiary structure checkpoint at anticodon loop modification in tRNA functional maturation,” Nat Struct Mol Biol, vol. 16, no. 10, pp. 1109–1115, Oct. 2009, doi: 10.1038/nsmb.1653.
P. Seelam Prabhakar, N. A. Takyi, and S. D. Wetmore, “Post-transcriptional modifications at the 37 th position in the anticodon stem loop of tRNA: Structural insights from MD simulations,” 2021. doi: doi: 10.1261/rna.078097.120.
G. Cho, J. Lee, and J. Kim, “Identification of a novel 5-Aminomethyl-2-Thiouridine methyltransferase in tRNA modification,” Nucleic Acids Res, vol. 51, no. 4, pp. 1971–1983, Feb. 2023, doi: 10.1093/nar/gkad048.
H. M. Berman et al., “The Protein Data Bank,” 2000. [Online]. Available: http://www.rcsb.org/pdb/status.html
M. D. Hanwell, D. E. Curtis, D. C. Lonie, T. Vandermeersch, E. Zurek, and G. R. Hutchison, “SOFTWARE Open Access Avogadro: an advanced semantic chemical editor, visualization, and analysis platform,” 2012. [Online]. Available: http://www.jcheminf.com/content/4/1/17
D. S. Goodsell and A. J. Olson, “Automated Docking of Substrates to Proteins by Simulated Annealing,” 1990.
N. P. S. Oktaviani, A. L. Ivansyah, M. Y. Saputra, N. Handayani, N. Fadylla, and D. Wahyuningrum, “Potential application of bisoprolol derivative compounds as antihypertensive drugs: Synthesis and in silico study,” R Soc Open Sci, vol. 10, no. 12, Dec. 2023, doi: 10.1098/rsos.231112.
P. Shifeng et al., “Molecular Docking and Dynamics Simulation Studies of Ginsenosides with SARS-CoV-2 Host and Viral Entry Protein Targets,” Nat Prod Commun, vol. 17, no. 11, Nov. 2022, doi: 10.1177/1934578X221134331.
D. Krewski et al., “Toxicity testing in the 21st century: A vision and a strategy,” Journal of Toxicology and Environmental Health - Part B: Critical Reviews, vol. 13, no. 2–4. pp. 51–138, Feb. 2010. doi: 10.1080/10937404.2010.483176.
DOI: 10.33751/helium.v4i1.10284
Abstract views : 92
views : 57
Refbacks
- There are currently no refbacks.
