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

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 o...

Full description

Saved in:
Bibliographic Details
Published in:Natural product research 2024-06, Vol.38 (12), p.2031-2039
Main Authors: Wang, An-Qi, Wang, Ya-Jie, Zhang, Jing, Fan, Yi-Ming, Li, Shi-Yang, Zou, Li-Wei
Format: Article
Language:English
Subjects:
Animals
Comparative studies
Enzyme Inhibitors - chemistry
Enzyme Inhibitors - pharmacology
Ginsenosides
Ginsenosides - chemistry
Ginsenosides - pharmacology
human pancreatic lipase
Humans
Hydrogen bonding
Hydrogen bonds
Hydrolysis
inhibitors
Kinetics
Lipase
Lipase - antagonists & inhibitors
Lipase - metabolism
Molecular docking
Molecular Docking Simulation
Molecular Structure
obesity
Pancreas
Pancreas - drug effects
Pancreas - enzymology
Structure-Activity Relationship
Structure-activity relationships
Swine
Citations: Items that this one cites
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:1478-6419
1478-6427
DOI:10.1080/14786419.2023.2235713