In Silico Evaluation of Bioactive Compounds from Caesalpinia sappan L. as Lipase and Penicillin-Binding Protein Inhibitors for Antibacterial Therapy

Andi Trihadi Kusuma, Andi Sitti Fahirah Arsal

Abstract


The increasing prevalence of antibiotic-resistant bacteria has created an urgent demand for alternative antibacterial agents with distinct molecular targets. Natural compounds derived from medicinal plants continue to play an important role in early drug discovery. Caesalpinia sappan contains diverse phenolic and flavonoid constituents with potential pharmacological activity. This study investigated selected bioactive compounds from sappan wood, excluding brazilein, as potential inhibitors of bacterial lipase and penicillin-binding protein (PBP) through computational analysis. Molecular docking was employed to examine binding affinity and protein–ligand interactions, while pharmacokinetic and toxicity properties were predicted using pkCSM. The docking results revealed that sappanchalcone showed the strongest interaction with bacterial lipase, whereas protosappanin A demonstrated the highest affinity toward PBP. Both compounds formed stable interactions with important active-site residues associated with enzymatic function. In addition, ADMET prediction indicated favorable pharmacokinetic characteristics, including adequate intestinal absorption, minimal toxicity, and low potential for cytochrome P450 inhibition. Overall, the findings indicate that sappanchalcone and protosappanin A may serve as promising multi-target antibacterial candidates and provide a computational basis for future experimental validation and antibacterial drug development.

Keywords


Caesalpinia sappan L.; molecular docking; lipase; penicillin-binding protein; antibacterial

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References


Banik, S., Pérez-Lemus, G.R., Kumar, S. Antibacterial potential of plant-derived flavonoids: a molecular docking perspective. Journal of Biomolecular Structure and Dynamics, 2020; 38(15): 4531–4545.

Berman, H.M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T.N., Weissig, H., Bourne, P.E. The Protein Data Bank. Nucleic Acids Research, 2000; 28(1): 235–242.

Cushnie, T.P.T., Lamb, A.J. Recent advances in understanding the antibacterial properties of flavonoids. International Journal of Antimicrobial Agents, 2011; 38(2): 99–107.

Daina, A., Michielin, O., Zoete, V. SwissADME: a free web tool to evaluate pharmacokinetics. Scientific Reports, 2017; 7: 42717.

Ghuysen, J.M. Serine β-lactamases and penicillin-binding proteins. Annual Review of Microbiology, 1991; 45: 37–67.

Jamal, M., Ahmad, W., Andleeb, S., et al. Bacterial biofilm and associated infections. Journal of the Chinese Medical Association, 2018; 81(1): 7–11.

Kim, S., Chen, J., Cheng, T., et al. PubChem in 2021. Nucleic Acids Research, 2021; 49(D1): D1388–D1395.

Pires, D.E.V., Blundell, T.L., Ascher, D.B. pkCSM. Journal of Medicinal Chemistry, 2015; 58(9): 4066–4072.

Silver, L.L. Challenges of antibacterial discovery. Clinical Microbiology Reviews, 2011; 24(1): 71–109.

Trott, O., Olson, A.J. AutoDock Vina. Journal of Computational Chemistry, 2010; 31(2): 455–461.

Wang, Z., Wang, D., Zhang, Y., Wang, L. Antibacterial activity of flavonoids. Frontiers in Microbiology, 2018; 9: 1763.

Xie, Y., Yang, W., Tang, F., Chen, X., Ren, L. Structure–activity relationship of flavonoids. Current Medicinal Chemistry, 2015; 22(1): 132–149.




DOI: https://doi.org/10.33096/pharmrep.v5i1.404

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Laboratory of Pharmaceutical Chemistry, Faculty of Pharmacy
Universitas Muslim Indonesia, Jl. Urip Sumohardjo KM 5 Kampus II, Makassar 90231, Indonesia
pharmaceutical.reports@umi.ac.id 

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