Evaluation of protein kinase c inhibition of ethyl-p-methoxycinnamate isolated from Kaempferia galanga L.
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Abstract
Objective: This study aimed to evaluate the inhibitory activity of the protein kinase C (PKC) enzyme by ethyl-p-methoxycinnamate (EPMC), a compound isolated from the dried rhizomes of Kaempferia galanga L., at three test concentrations: 50 µM, 100 µM, and 150 µM.
Subjects and methods: EPMC was extracted using ultrasound-assisted extraction and purified by recrystallization with a n-hexane:methanol (1:1, v/v) solvent system. Its structure and purity were confirmed by thin-layer chromatography (TLC), proton and carbon nuclear magnetic resonance spectroscopy (¹H-NMR and ¹³C-NMR), and melting point analysis. The inhibitory activity against PKC was evaluated using the ELISA method.
Results: The isolated EPMC showed high purity and clearly identified chemical structure. ELISA assay results demonstrated that EPMC significantly inhibited PKC activity from Candida albicans, with the most pronounced effect observed at 100 µM.
Conclusion: These findings suggest that EPMC may serve as a promising candidate for modulating PKC-related signaling pathways in Candida albicans.
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References
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