Scopoletin and Morin Inhibit Lactate Dehydrogenase Enzyme Activity, Which Is Critical for Cancer Metabolism
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Article Type:
Research/Original Article (دارای رتبه معتبر)
Abstract:
Background
Lactate dehydrogenase (LDH) is a tetrameric enzyme that catalyzes the interconversion of pyruvate to L-lactate. The importance of this enzyme is because LDH isoenzymes are involved in cancer, heart, and liver diseases. Inhibition of this enzyme can help prevent and treat different diseases. Morin is a flavonoid found in the Moraceae family and scopoletin is a coumarin found in Scopolia genus.
Objectives
The aim of this study was to determine the effect of morin and scopoletin as two natural products on the activity and structure of lactate dehydrogenase enzyme.
Methods
Morin and scopoletin were examined for inhibition of the activity of LDH in 100 mM sodium phosphate buffer pH 7.5, at room temperature using UV-V spectrophotometry. Fluorescence spectroscopy was used to characterize protein structural changes in the presence of morin and scopoletin.
Results
Km and Vmax of LDH for pyruvate were 11.69 mM and 1.258 mM/min, respectively. The kinetic results showed that morin and scopoletin are LDH inhibitors. The Ki values of morin and scopoletin were determined as 1.78 µM and 0.8 µM, respectively, using a secondary plot. Fluorescence intensity quenching and red shift of the maximum wavelength of emission in a concentration-dependent manner showed that morin and scopoletin bind to LDH and affect its structure.
Conclusions
The results suggest that morin and scopoletin bind to LDH, influence its conformation and inhibit its activity. Scopoletin showed more effective inhibition of LDH activity and it can be a promising candidate in the field of tumor metabolism inhibitors.
Language:
English
Published:
Hormozgan Medical Journal, Volume:23 Issue: 1, Jan-Mar 2019
Page:
1
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