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Effect of Compounds from Moringa oleifera Lam. on in Vitro Non‐Alcoholic Fatty Liver Disease (NAFLD) Model System
Author(s) -
Ukiya Motohiko,
Motegi Kazuki,
Sato Daisuke,
Kimura Hirokazu,
Satsu Hideo,
Koketsu Mamoru,
Ninomiya Masayuki,
Myint Lwin Mon,
Nishina Atsuyoshi
Publication year - 2021
Publication title -
chemistry and biodiversity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.427
H-Index - 70
eISSN - 1612-1880
pISSN - 1612-1872
DOI - 10.1002/cbdv.202100243
Subject(s) - moringa , fatty liver , chemistry , fenofibrate , intracellular , fatty acid , lipolysis , biochemistry , pharmacology , medicine , disease , adipose tissue , biology , food science
Non‐alcoholic fatty liver disease (NAFLD) is currently the most common chronic liver disease in the world, with a prevalence of 25 % in many countries. To date, no drug has been approved to treat NAFLD, therefore, the use of phytochemicals to prevent this disease is meaningful. In this study, we focused on the effects of Moringa oleifera Lam. on diabetes, attempted to isolate compounds that regulate NAFLD. Compounds 1 and 2 were isolated from the ethyl acetate fraction of M. oleifera . Spectral data revealed that they were 1‐hydroxy‐3‐phenylpropan‐2‐yl benzoate ( 1 ) and benzyl benzylcarbamate ( 2 ), respectively. The three‐dimensional structure of compound 1 was determined by single crystal X‐ray structural analysis. Neither compound was toxic to HepG2 cells, and compound 1 was found to have a concentration‐dependent inhibitory effect on intracellular lipid accumulation induced by stimulation of linoleic acid (LA). As a result of measuring the effects of compound 1 on the intracellular lipid production‐related protein, it was found that compound 1 enhanced protein expression that promotes lipolysis. On the other hand, since the action of compound 1 was similar to that of PPARα agonists, it is deduced that compound 1 enhanced the activity of PPARα and further enhanced the expression of lipolytic proteins, which is related to the suppression of intracellular lipid accumulation. Furthermore, as the result of docking simulation, compound 1 had a higher binding affinity to the ligand binding site of PPARα than fenofibrate, which is a PPARα agonist, and thus compound 1 was considered to be promising as an agonist of PPARα.