scholarly journals In-vitro functional efficacy of extracts from Caucasian Rhododendron (Rhododendron caucasicum) and Rkatsiteli wines as pancreatic lipase inhibitors

2021 ◽  
Vol 10 (1) ◽  
pp. 37-50
Author(s):  
Zhuzha Khatchapuridze ◽  
Givi Gugulashvili ◽  
Vitali Ghvachliani ◽  
Angelika Ploeger ◽  
Levan Gulua ◽  
...  
Keyword(s):  
Pancreatic Lipase ◽  
Pancreatic Lipase Inhibitors

In silico identification and in vitro activity of new pancreatic lipase inhibitors

Planta Medica ◽  
2016 ◽  
Vol 81 (S 01) ◽  
pp. S1-S381
Author(s):  
T Buchholz ◽  
A Frank ◽  
G Wolber ◽  
MF Melzig
Keyword(s):  
Pancreatic Lipase ◽  
In Silico ◽  
Vitro Activity ◽  
In Vitro Activity ◽  
In Silico Identification ◽  
Pancreatic Lipase Inhibitors

scholarly journals Pancreatic Lipase Inhibitory Alkaloids of Murraya koenigii Leaves

2009 ◽  
Vol 4 (8) ◽  
pp. 1934578X0900400 ◽  
Author(s):  
Rahul Birari ◽  
Somendu Kumar Roy ◽  
Anubha Singh ◽  
Kamlesh Kumar Bhutani
Keyword(s):  
Pancreatic Lipase ◽  
Inhibitory Activity ◽  
Murraya Koenigii ◽  
Etoac Extract ◽  
Inhibitory Potential ◽  
Pancreatic Lipase Inhibitors ◽  
First Time ◽  
Carbazole Alkaloids

In the continuing search for newer pancreatic lipase inhibitors from plants, a total of 63 extracts from 21 different plants were screened to study their pancreatic lipase (PL) inhibitory activity in vitro. All three extracts (DCM, EtOAc and MeOH) of Murraya koenigii (L.) Spreng leaves (Rutaceae) exhibited antilipase activity greater than 80%. Further, bioactivity guided fractionation of the EtOAc extract led to the isolation of four alkaloids, namely mahanimbin, koenimbin, koenigicine and clausazoline-K, with IC50 values of 17.9 μM, 168.6 μM, 428.6 μM and ≤500 μM, respectively. This study reports for the first time the PL inhibitory potential of carbazole alkaloids from plants.

A review on pancreatic lipase inhibitors from natural sources: a potential target for obesity

2021 ◽  
Vol 17 ◽  
Author(s):  
Bency Baby T ◽  
Murali R ◽  
Suriyaprakash TNK ◽  
Srinivasan N
Keyword(s):  
Natural Products ◽  
Pancreatic Lipase ◽  
Inhibitory Activity ◽  
Journal Article ◽  
Natural Sources ◽  
Potential Target ◽  
Biological Sources ◽  
Pancreatic Lipase Inhibitors

Background: Obesity is a worldwide lifestyle disorder and its incidence is growing at an alarming rate. Pancreatic lipase (PL) plays a key role in lipid metabolism and hence a potential target for obesity treatment. There have been reports that many bioactive compounds from natural sources are vast pool of PL inhibitors. Objective: In search of natural pancreatic lipase inhibitors, the review summarizes the potential of natural products for their pancreatic lipase inhibitory activity. Methods: In this review the data obtained from literature search across various electronic databases and journal article publications are reviewed. Results: The pancreatic lipase inhibitory activities of 61 biological sources were reviewed in this paper is backed by preclinical experimental evidence, either in vivo or in vitro. Conclusion: This article can be used as a ready to use reference for therapeutic lead molecules from plants, marine and insect derived natural products with PL inhibitory activity. The research is more focused on the discovery of more ingenious pancreatic lipase inhibitors with lesser consequences.

scholarly journals Inhibition of pancreatic lipase in vitro by the covalent inhibitor tetrahydrolipstatin

1988 ◽  
Vol 256 (2) ◽  
pp. 357-361 ◽  
Author(s):  
P Hadváry ◽  
H Lengsfeld ◽  
H Wolfer
Keyword(s):  
Transition State ◽  
Acid Derivative ◽  
Pancreatic Lipase ◽  
Active Site ◽  
Boronic Acid ◽  
Selective Inhibitor ◽  
Covalent Intermediate ◽  
State Form ◽  
Covalent Inhibitor

Tetrahydrolipstatin inhibits pancreatic lipase from several species, including man, with comparable potency. The lipase is progressively inactivated through the formation of a long-lived covalent intermediate, probably with a 1:1 stoichiometry. The lipase substrate triolein and also a boronic acid derivative, which is presumed to be a transition-state-form inhibitor, retard the rate of inactivation. Therefore, in all probability, tetrahydrolipstatin reacts with pancreatic lipase at, or near, the substrate binding or active site. Tetrahydrolipstatin is a selective inhibitor of lipase; other hydrolases tested were at least a thousand times less potently inhibited.

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