Panduratin A is an orally active natural compound with multiple pharmacological activities. By specifically inhibiting the NF-κB signaling pathway, Panduratin A exerts potent anti-inflammatory and antioxidant effects in intestinal and vascular inflammation models. Panduratin A exerts a definite protective effect against Colistin -induced nephrotoxicity by alleviating oxidative stress, improving mitochondrial dysfunction and inhibiting cell apoptosis. Panduratin A activates autophagy via an AMPK -dependent pathway and exhibits anti-tuberculosis activity. Panduratin A exerts antiviral effects by inhibiting the methyltransferase ( DNA Methyltransferase ) of SARS-CoV-2 [1] [2] [3] [4] [5].
In Vivo, Panduratin A (3-18 mg/kg; p.o.; daily; 14 days) dose-dependently mitigates DSS -induced ulcerative colitis in male mice[1]. Panduratin A reduces SARS-CoV-2 viral burden and lung inflammation in infected Golden Syrian hamsters[3]. Panduratin A (2.5-25 mg/kg; i.p.; daily; 7 days) exerts dose-dependent nephroprotective effects against Colistin-induced acute kidney injury by reducing oxidative stress, renal tubular damage, and renal cell apoptosis[5].
In Vitro, Panduratin A alleviates tert-butyl hydroperoxide-induced oxidative damage in human hepatocellular carcinoma (HepG2) cells[1]. Panduratin A inhibits the production of inflammatory mediators TNF-α, NO and PGE2 in vitro[1]. Panduratin A inhibits mast cell degranulation and cytokine expression in rat basophilic leukemia mast cells[1]. Panduratin A (0.5-10 μM; 48 h) shows no toxicity to HMEC-1 human endothelial cells, and the cell viability remains above 90% at concentrations up to 4 μM (48 h treatment)[2]. Panduratin A (2-4 μM; 27 h) reduces the secretion levels of IL-6 and MCP-1 in TNF-α-stimulated human endothelial cell line HMEC-1 in a dose-dependent manner, with the strongest effect observed at 4 μM[2]. Panduratin A (4 μM; 24 h) inhibits TNF-α-induced upregulation of VCAM-1 and ICAM-1 in human endothelial cell line HMEC-1, while preserving cell morphology and cytoskeletal structure[2]. Panduratin A (4 μM; 24 h) significantly reduces the adhesion of THP-1 human monocytes to TNF-α-stimulated HMEC-1 human endothelial cells[2]. Panduratin A (2-4 μM; 3.5 h) dose-dependently inhibits TNF-α-induced phosphorylation of NF-κB and degradation of IκB in human endothelial cell line HMEC-1, with the most potent effect observed at 4 μM[2]. Panduratin A (2-4 μM; 3.5 h) dose-dependently inhibits TNF-α-induced NF-κB nuclear translocation and maintains the cytoplasmic IκB level in HMEC-1 human endothelial cells[2]. Panduratin A (50 μM; 4 h) induces autophagosome formation in RAW264.7 macrophages[3]. Panduratin A (0.048-50 μM; 2 h) acts as an autophagy inducer in RAW264.7 macrophages, with an EC50 of 12.55 μM; this is evidenced by the dose-dependent increase in the LC3-II/actin ratio and the dose-dependent decrease in the p62/actin ratio[3]. Panduratin A (25 μM; 4 h) induces complete autophagic flux in RAW264.7 macrophages, which is characterized by increased numbers of both autophagosomes and autolysosomes, as well as regulation of autophagic marker protein levels[3]. Panduratin A (25 μM; 4 h) induces autophagy in RAW264.7 macrophages via activating AMPK, independent of the inhibitory effect on the mTOR signaling pathway[3]. Panduratin A (25 μM; 2-24 h) does not induce TFEB nuclear translocation in RAW264.7 macrophages, which is consistent with mTOR-independent autophagy induction[3]. Panduratin A (1.5625-50 μM; 24 h) inhibits the survival of Mtb within RAW264.7 macrophages in a dose-dependent manner via a host-mediated mechanism rather than direct mycobactericidal activity, and this effect is significant when treated at 25 and 50 μM for 24 h[3]. Panduratin A (25 μM; 24 h) inhibits Mtb survival in RAW264.7 macrophages in a Beclin-1-dependent manner, suggesting that it mediates bacterial clearance via autophagy[3]. Panduratin A (25 μM; 4 h) enhances the sequestration of Mtb into autophagosomes in RAW264.7 macrophages[3]. Panduratin A (25 μM; 4 h) promotes autophagy-dependent trafficking of Mtb to lysosomes in RAW264.7 macrophages[3]. Panduratin A (1-5 μM) protects RPTEC/TERT1 cells against polymyxin-induced toxic damage by increasing cell viability, reducing apoptosis and reactive oxygen species (ROS) production, maintaining mitochondrial membrane potential, upregulating the anti-apoptotic protein Bcl-2, and downregulating the pro-apoptotic protein cytochrome c and activated caspase-3, with the most significant effect observed at the concentration of 5 μM[5].
References:
[1]. Alqudah A, et al. Panduratin A mitigates inflammation and oxidative stress in DSS-induced colitis mice model. Future Sci OA. 2024;10(1):2428129.
[2]. Kiatsoonthon K, et al. Panduratin A Inhibits TNF Alpha-Stimulated Endothelial Cell Activation Through Suppressing the NF-κB Pathway. Biomolecules. 2024;15(1):34. Published 2024 Dec 30.
[3]. Lamtha T, et al. Panduratin A Induces Autophagy Through AMPK Activation Independent of mTOR Inhibition and Restricts Mycobacterium tuberculosis in Host Macrophages. Mol Microbiol. 2025;124(6):491-506.
[4]. Boonserm P, et al. A computational study on the molecular mechanisms of panduratin A as a potential inhibitor on SARS-CoV-2 protein targets. Heliyon. 2023;9(1):e12780.
[5]. Worakajit N, et al. Nephroprotective potential of Panduratin A against colistin-induced renal injury via attenuating mitochondrial dysfunction and cell apoptosis. Biomed Pharmacother. 2022;148:112732.
In Vivo, Panduratin A (3-18 mg/kg; p.o.; daily; 14 days) dose-dependently mitigates DSS -induced ulcerative colitis in male mice[1]. Panduratin A reduces SARS-CoV-2 viral burden and lung inflammation in infected Golden Syrian hamsters[3]. Panduratin A (2.5-25 mg/kg; i.p.; daily; 7 days) exerts dose-dependent nephroprotective effects against Colistin-induced acute kidney injury by reducing oxidative stress, renal tubular damage, and renal cell apoptosis[5].
In Vitro, Panduratin A alleviates tert-butyl hydroperoxide-induced oxidative damage in human hepatocellular carcinoma (HepG2) cells[1]. Panduratin A inhibits the production of inflammatory mediators TNF-α, NO and PGE2 in vitro[1]. Panduratin A inhibits mast cell degranulation and cytokine expression in rat basophilic leukemia mast cells[1]. Panduratin A (0.5-10 μM; 48 h) shows no toxicity to HMEC-1 human endothelial cells, and the cell viability remains above 90% at concentrations up to 4 μM (48 h treatment)[2]. Panduratin A (2-4 μM; 27 h) reduces the secretion levels of IL-6 and MCP-1 in TNF-α-stimulated human endothelial cell line HMEC-1 in a dose-dependent manner, with the strongest effect observed at 4 μM[2]. Panduratin A (4 μM; 24 h) inhibits TNF-α-induced upregulation of VCAM-1 and ICAM-1 in human endothelial cell line HMEC-1, while preserving cell morphology and cytoskeletal structure[2]. Panduratin A (4 μM; 24 h) significantly reduces the adhesion of THP-1 human monocytes to TNF-α-stimulated HMEC-1 human endothelial cells[2]. Panduratin A (2-4 μM; 3.5 h) dose-dependently inhibits TNF-α-induced phosphorylation of NF-κB and degradation of IκB in human endothelial cell line HMEC-1, with the most potent effect observed at 4 μM[2]. Panduratin A (2-4 μM; 3.5 h) dose-dependently inhibits TNF-α-induced NF-κB nuclear translocation and maintains the cytoplasmic IκB level in HMEC-1 human endothelial cells[2]. Panduratin A (50 μM; 4 h) induces autophagosome formation in RAW264.7 macrophages[3]. Panduratin A (0.048-50 μM; 2 h) acts as an autophagy inducer in RAW264.7 macrophages, with an EC50 of 12.55 μM; this is evidenced by the dose-dependent increase in the LC3-II/actin ratio and the dose-dependent decrease in the p62/actin ratio[3]. Panduratin A (25 μM; 4 h) induces complete autophagic flux in RAW264.7 macrophages, which is characterized by increased numbers of both autophagosomes and autolysosomes, as well as regulation of autophagic marker protein levels[3]. Panduratin A (25 μM; 4 h) induces autophagy in RAW264.7 macrophages via activating AMPK, independent of the inhibitory effect on the mTOR signaling pathway[3]. Panduratin A (25 μM; 2-24 h) does not induce TFEB nuclear translocation in RAW264.7 macrophages, which is consistent with mTOR-independent autophagy induction[3]. Panduratin A (1.5625-50 μM; 24 h) inhibits the survival of Mtb within RAW264.7 macrophages in a dose-dependent manner via a host-mediated mechanism rather than direct mycobactericidal activity, and this effect is significant when treated at 25 and 50 μM for 24 h[3]. Panduratin A (25 μM; 24 h) inhibits Mtb survival in RAW264.7 macrophages in a Beclin-1-dependent manner, suggesting that it mediates bacterial clearance via autophagy[3]. Panduratin A (25 μM; 4 h) enhances the sequestration of Mtb into autophagosomes in RAW264.7 macrophages[3]. Panduratin A (25 μM; 4 h) promotes autophagy-dependent trafficking of Mtb to lysosomes in RAW264.7 macrophages[3]. Panduratin A (1-5 μM) protects RPTEC/TERT1 cells against polymyxin-induced toxic damage by increasing cell viability, reducing apoptosis and reactive oxygen species (ROS) production, maintaining mitochondrial membrane potential, upregulating the anti-apoptotic protein Bcl-2, and downregulating the pro-apoptotic protein cytochrome c and activated caspase-3, with the most significant effect observed at the concentration of 5 μM[5].
References:
[1]. Alqudah A, et al. Panduratin A mitigates inflammation and oxidative stress in DSS-induced colitis mice model. Future Sci OA. 2024;10(1):2428129.
[2]. Kiatsoonthon K, et al. Panduratin A Inhibits TNF Alpha-Stimulated Endothelial Cell Activation Through Suppressing the NF-κB Pathway. Biomolecules. 2024;15(1):34. Published 2024 Dec 30.
[3]. Lamtha T, et al. Panduratin A Induces Autophagy Through AMPK Activation Independent of mTOR Inhibition and Restricts Mycobacterium tuberculosis in Host Macrophages. Mol Microbiol. 2025;124(6):491-506.
[4]. Boonserm P, et al. A computational study on the molecular mechanisms of panduratin A as a potential inhibitor on SARS-CoV-2 protein targets. Heliyon. 2023;9(1):e12780.
[5]. Worakajit N, et al. Nephroprotective potential of Panduratin A against colistin-induced renal injury via attenuating mitochondrial dysfunction and cell apoptosis. Biomed Pharmacother. 2022;148:112732.