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Hormozgan Medical Journal، جلد ۲۳، شماره ۱، صفحات ۰-۰
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| عنوان فارسی |
Scopoletin and Morin Inhibit Lactate Dehydrogenase Enzyme Activity, Which Is Critical for Cancer Metabolism |
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| چکیده فارسی مقاله |
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 concentrationdependent 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. |
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| کلیدواژه‌های فارسی مقاله |
Lactate Dehydrogenase،Morin،Scopoletin،Spectrophotometry،Enzyme inhibitors، |
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| عنوان انگلیسی |
Scopoletin and Morin Inhibit Lactate Dehydrogenase Enzyme Activity, Which Is Critical for Cancer Metabolism |
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| چکیده انگلیسی مقاله |
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 concentrationdependent 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. |
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| کلیدواژه‌های انگلیسی مقاله |
Lactate Dehydrogenase,Morin,Scopoletin,Spectrophotometry,Enzyme inhibitors |
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| نویسندگان مقاله |
| Melika Mazlaghaninia
| Maliheh Sadat Atri
| Bagher Seyedalipour
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| نشانی اینترنتی |
http://hmj.hums.ac.ir/browse.php?a_code=A-10-2-1223&slc_lang=en&sid=1 |
| فایل مقاله |
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| کد مقاله (doi) |
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| زبان مقاله منتشر شده |
en |
| موضوعات مقاله منتشر شده |
عمومی |
| نوع مقاله منتشر شده |
پژوهشی |
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