4.4 Article

Comparative study on inhibitory effects of ginsenosides on human pancreatic lipase and porcine pancreatic lipase: structure-activity relationships and inhibitory mechanism

Journal

NATURAL PRODUCT RESEARCH
Volume -, Issue -, Pages -

Publisher

TAYLOR & FRANCIS LTD
DOI: 10.1080/14786419.2023.2235713

Keywords

Ginsenosides; human pancreatic lipase; inhibitors; structure-activity relationships; obesity; >

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The inhibitory effects of twenty-six ginsenosides on human pancreatic lipase (hPL) and porcine pancreatic lipase (pPL) were studied. It was found that nine ginsenosides have moderate inhibitory effects on hPL, with good selectivity over pPL. In contrast, (S)-Rh2 exhibited good inhibitory effects on pPL over hPL. SAR analysis indicated that the introduction of the O-glycosyl group(s) at the C-3/C-7 site is not beneficial for hPL inhibition, and ginsenosides with the A-skeleton are more beneficial compared to those with the B-/C-skeleton. Inhibition kinetic analysis revealed that Rg3 and (S)-Rh2 inhibit hPL-catalyzed DDAO-ol hydrolysis in a mixed manner. Molecular docking studies confirmed that Rg3 and (S)-Rh2 inhibit hPL by forming multiple Pi-hydrogen interactions and hydrogen bonds with catalytic residues of hPL. These findings highlight the importance of using hPL rather than pPL to evaluate the inhibitory effect of PL.
The inhibitory effects of twenty-six ginsenosides on human pancreatic lipase (hPL) and porcine pancreatic lipase (pPL) were studied. Study reveals that nine ginsenosides have moderate inhibitory effects against hPL, and good selectivity over pPL. By contrast, (S)-Rh2 showed good inhibitory effects on pPL over hPL. SAR analysis indicated that introduction of the O-glycosyl group(s) at C-3/C-7 site is unbeneficial for hPL inhibition, ginsenosides with A-skeleton is more beneficial than ginsenosides with B-/C-skeleton. Inhibition kinetic analysis indicated that Rg3 and (S)-Rh2 inhibited hPL-catalyzed DDAO-ol hydrolysis in a mixed manner. Molecular docking studies have confirmed that Rg3 and (S)-Rh2 inhibit hPL via many Pi-hydrogen interactions and hydrogen bonds with catalytic residues of hPL. These results indicated that pPL as an enzyme source could not fully represent the inhibitory effect of the tested compounds on hPL, and hPL should be used as far as possible to evaluate the inhibitory effect of PL.

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