Journal articles: 'Pancreatic lipase inhibitor'

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Winanda, Witri, Irmanida Batubara, and Yulin Lestari. "Pancreatic Lipase Inhibitory Activity of Endophytic Actinobacteria from Rhododendron spp." Biosaintifika: Journal of Biology & Biology Education 13, no. 2 (August 30, 2021): 178–84. http://dx.doi.org/10.15294/biosaintifika.v13i2.29981.

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Antiobesity medication is available as therapeutic compounds that can reduce fat digestion by the inhibition of pancreatic lipase. Actinobacteria have the potency as source of bioactive compounds with various biological function including as pancreatic lipase inhibitor. However, the potency of endophytic actinobacteria from Rhododendron spp. as source of pancreatic lipase inhibitor producer has not been reported yet. The aim of this study was to examine the potential of pancreatic lipase inhibitory activity of 23 endophytic actinobacteria from Rhododendron spp.; to characterize their colony based on morphology and molecular analysis. Screening test of pancreatic lipase inhibitor was conducted using the supernatant of endophytic actinobacteria, lipase pancreatic porcine (L3126) and p-nitrophenyl butyrate. The supernatant of selected isolates was extracted using ethyl acetate. The result showed that various inhibitory activities ranging between 0.00 until 91.69%. There were 11 out of 23 isolates that have potential as pancreatic inhibitor. Amongst them, the extract of four selected isolates, i.e. RZP 1.3, RSSB 3.2, RSS 2.1, and RJB F3.2 demonstrated inhibitory percentage of more than 80%. The RJB F3.2 extract showed to have IC50 value by 431.48 µg mL-1 compared to control, i.e. Xenical (89.07 µg mL-1). Phytochemical analysis exhibited that the extract of the selected isolates contained alkaloid which may function as pancreatic lipase inhibitor. Based on the morphological character, the selected isolates have various morphological colonies and 16S rRNA gene sequence revealed the sequence homology to Streptomyces spp. The data clearly indicate that endophytic actinobacteria from Rhododendron spp. have potency as pancreatic lipase inhibitor producer and further studies could be explored for the development of antiobesity agent.

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Mhatre, Sveeta V., Amita A. Bhagit, and Raman P. Yadav. "Proteinaceous Pancreatic Lipase Inhibitor from the Seed of Litchi chinensis." Food technology and biotechnology 57, no. 1 (2019): 113–18. http://dx.doi.org/10.17113/ftb.57.01.19.5909.

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A study of the pancreatic lipase inhibitory activity of a protein from the seed of Litchi chinensis was carried out. Protein was isolated by 70 % ammonium sulphate precipitation followed by dialysis. Lipase inhibitory activity of the protein was evaluated using both synthetic (p-nitrophenyl palmitate) and natural (olive oil) substrates. Protein at the final concentration of 100 µg/mL was able to inhibit 68.2 % pancreatic lipase on synthetic substrate and 60.0 % on natural substrate. Proteinaceous nature of the inhibitor was determined using trypsinization assay. Pancreatic lipase inhibitory protein was sensitive to 0.05 % trypsin treatment with the loss of 61.9 % activity. IC50 of this proteinaceous pancreatic lipase inhibitor was 73.1 µg/mL using synthetic substrate. This inhibitory protein was sensitive to pH, with the highest inhibitory activity at pH=8.0 and the lowest at pH=3.0. Protein was further analyzed using 10 % non-reducing sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and, interestingly, it showed the presence of a single band of (61±2) kDa when stained with Coomassie brilliant blue. The isolated protein was finally crystallized to see its homogeneity by batch crystallization method. Crystals were well formed with distinct edges. The isolated protein showed good pancreatic lipase inhibitory activity.

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Hou, W., Y. Arita, and J. Morisset. "Caerulein-stimulated arachidonic acid release in rat pancreatic acini: a diacylglycerol lipase affair." American Journal of Physiology-Cell Physiology 271, no. 5 (November 1, 1996): C1735—C1742. http://dx.doi.org/10.1152/ajpcell.1996.271.5.c1735.

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This study was performed to evaluate the effect of caerulein, a cholecystokinin analogue, on arachidonic acid (AA) release in rat pancreatic acini and to determine the cellular mechanism involved. Caerulein did not stimulate phospholipase A2 (PLA2); however, diacylglycerol (DAG) lipase activity was increased. Validity of PLA2 or DAG lipase inhibitors was confirmed by their ability to selectively inhibit PLA2 or DAG lipase activities. Caerulein increased AA release from acini prelabeled with [3H]AA both dose and time dependently. Inhibitors were used to evaluate the involvement of different signaling pathways. Mepacrine and aristolochic acid, two PLA2 inhibitors, did not inhibit caerulein-induced AA release, whereas the DAG lipase inhibitor RHC-80267 did. The phospholipase C (PLC) inhibitor U-73122 totally inhibited caerulein-induced AA release, whereas the phospholipase D (PLD) inhibitor wortmannin had no effect. Our data indicate that caerulein-induced AA release results from the combined action of PLC and DAG lipase without PLA2 or PLD activation.

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ALAGÖZ, Mehmet Abdullah, İnci Selin DOĞAN, Sıla SENER, and Zeynep ÖZDEMİR. "Synthesis, Molecular Docking and Molecular Dynamics Simulation Studies of Some Pyridazinone Derivatives as Lipase Inhibitors." Cumhuriyet Science Journal 43, no. 3 (September 30, 2022): 391–97. http://dx.doi.org/10.17776/csj.1135400.

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Human health and illness are dependent on lipases, which play a key role in maintaining cell integrity, storing fat for energy and serving as signaling molecules. In this study, 4 compounds that carry 6-phenylpyridazin-3(2H)-one main nucleus, which can be effective as lipase inhibitors, were synthesized and their structures were elucidated. The biological activity of synthesized compounds was evaluated via the porcine pancreatic lipase type II (PLL) inhibitor assay. Orlistat, a lipase inhibitor, was used as a positive control. Compound 8d was found to be the most effective compound, with an IC50 value of 32.66±2.8265 (μg/mL). In addition, molecular docking and molecular dynamics simulations studies were carried out to examine the interactions of the compounds with the target in detail. The results obtained as a result of these in silico studies were found to be compatible with the lipase inhibition effects of the compounds. It was observed that the compounds may have potential lipase inhibitory effects as a result of the substitutions of the 3-(6-oxo-3-phenylpyridazin-1(6H)-yl)propanehydrazide structure.

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Hadváry, P., H. Lengsfeld, and H. Wolfer. "Inhibition of pancreatic lipase in vitro by the covalent inhibitor tetrahydrolipstatin." Biochemical Journal 256, no. 2 (December 1, 1988): 357–61. http://dx.doi.org/10.1042/bj2560357.

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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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Li, Xuan, Sayo Morita, Hiroaki Yamada, Keita Koga, Wakana Ota, Toma Furuta, Atsushi Yamatsu, and Mujo Kim. "Free Linoleic Acid and Oleic Acid Reduce Fat Digestion and Absorption In Vivo as Potent Pancreatic Lipase Inhibitors Derived from Sesame Meal." Molecules 27, no. 15 (August 1, 2022): 4910. http://dx.doi.org/10.3390/molecules27154910.

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Pancreatic lipase catalyzes the cleavage of triacylglycerols at the oil–water interface, and is known as the dominant determiner of dietary fat digestion. Reducing dietary fat digestion and absorption by modulating the activity of pancreatic lipase has become a favorable strategy to tackle obesity. Orlistat is, at present, the only pancreatic lipase inhibitor approved for the treatment of obesity; however, an array of gastrointestinal adverse effects associated with orlistat limits its tolerability. As a safe alternative to orlistat, a number of natural product-derived compounds with varying degrees of pancreatic lipase inhibitory activity have been reported. We herein reported that bioactivity-guided fractionation of sesame meal led to the identification of free linoleic acid and oleic acid as potent inhibitors of porcine pancreatic lipase in vitro with an IC50 of 23.1 µg/mL (82.4 µM) and 11.7 µg/mL (41.4 µM), respectively. In rats, a single oral dose of the mixture of these fatty acids significantly suppressed the elevation of blood triacylglycerol level following fat intake. These results substantiate the role of free linoleic acid and oleic acid as a novel class of natural product-derived functional molecules that act as pancreatic lipase inhibitors, and their potential for healthy, routine-based weight management.

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Mhatre, S., A. Bhagit, and R. P. Yadav. "IN VITRO STUDIES OF SOME EDIBLE SPICES ON PANCREATIC LIPASE INHIBITORY ACTIVITY." INDIAN DRUGS 54, no. 02 (February 25, 2017): 62–68. http://dx.doi.org/10.53879/id.54.02.10815.

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Pancreatic lipase inhibitory effect of some edible spices in light of percent inhibition, efficacy, reversibility/ irreversibility and effect of pH on inhibition is presented here. Lipase inhibitory activities of methanolic extracts of eighteen spices were evaluated. Extracts of Zanthoxylum armatum, Cinnamomum tamala, Syzygium aromaticum and Myristica fragrans were considered to be of high potency in synthetic substrate assay. Only Syzygium aromaticum showed high potency in natural substrate based lipase assay. Zanthoxylum armatum extract displayed lowest IC50 of 9.0 μg/mL. On dialysis, all extracts lost their lipase inhibitory activity indicating reversible nature of inhibition. pH significantly affected the performance of spice extracts during inhibition of pancreatic lipase. Most of the extracts lost their pancreatic lipase inhibitory activity at pH 3.0 with the exception of Brassica nigra and Cinnamomum tamala. Results showed spice are good source of pancreatic lipase inhibitor and its potential as drug for obesity can be explored by addressing various issues.

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Rathod, Priyanka, Chandana Kulkarni, and Raman P. Yadav. "ANTI-DIABESITY PRINCIPLE FROM THE SEEDS OF PHYLLANTHUS EMBLICA L." INDIAN DRUGS 57, no. 12 (April 20, 2021): 41–50. http://dx.doi.org/10.53879/id.57.12.12323.

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In recent years, pancreatic lipase inhibitor and α- glucosidase inhibitor have been highlighted as potential anti-diabesity principles. In the present study, seeds of Phyllanthus emblica L. (Family: Phyllanthaceae) was studied for anti-diabesity potential in terms of pancreatic lipase inhibitory activity, α-glucosidase inhibitory activity and antioxidant activity. At 100μg/ml concentration, pancreatic lipase inhibition of the methanolic extract using synthetic substrate obtained was 73.2±0.1% (IC50 59.1μg/ml), whereas pancreatic lipase inhibition using natural substrate was 87.9 ± 2.62%. α- glucosidase inhibition of the extract at 50μg/ml was measured as 94.4±0.37% (IC50 34.4μg/ml). The superoxide scavenging activity of the extract was found to be 81.5±0.41%. Interestingly, upon TLC fingerprinting, only one band with Rf 0.70 showed multifunctional activity. The phytochemical found to be present was an alkaloid. The results evidenced the presence of multifunctional smart molecule in methanolic extract of P. emblica L and showed an alkaloid as the component responsible for anti-diabesity potential.

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Sari, Desi Ratna, Aurelia Afra, Erni Yupita Sari Br Sembiring, and Cico Jhon Karunia Simamora. "Fat-Rich Food Review on Obesity Control through Induction Enzyme Inhibitors." BIOEDUSCIENCE 5, no. 3 (December 31, 2021): 211–17. http://dx.doi.org/10.22236/j.bes/536903.

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Background: Obesity is an imbalance between height and weight due to excessive body fat tissue. The purpose of writing this review is to find out the effect of enzyme inhibitor induction on fat-rich foods as control of obesity. Method: Writing and assessing source problems related to using literature study methods. Results: One way of controlling obesity is by regulating dietary patterns and consumption of lipase inhibitors. Inhibition of lipase is one of the most widely developed effective ways in diet medicine. Inhibitory compounds cause pancreatic lipase to lose its ability in decomposition that enters the blood. The potency of plant-origin lipase inhibitor compounds can be increased in both number and performance. Increasing the production of secondary metabolite group inhibitors is by fermentation of microorganisms. Conclusion: Inhibition of triglyceride hydrolysis through inhibition of lipase enzymes can decrease and prevent obesity. Secondary metabolite induction can be fermented with microorganisms. The production of secondary metabolite compounds in medicinal plants can be increased in the presence of fermentation. Flavonoids can decrease the accumulation of lipids in the heart, reduce glucose absorption, inhibit the breakdown of polysaccharides into monosaccharides.

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Kato, Eisuke, Ai Tsuruma, Ayaka Amishima, and Hiroshi Satoh. "Proteinous pancreatic lipase inhibitor is responsible for the antiobesity effect of young barley (Hordeum vulgare L.) leaf extract." Bioscience, Biotechnology, and Biochemistry 85, no. 8 (May 28, 2021): 1885–89. http://dx.doi.org/10.1093/bbb/zbab096.

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ABSTRACT Young barley leaves (Hordeum vulgare L.) have various health effects and are employed as an ingredient in the production of health-promoting foods. Promoting antiobesity is one such health effect; however, the mechanism and bioactive compounds are unclear. In this research, young barley leaf extract (YB) was demonstrated to possess pancreatic lipase inhibitory activity. The addition of YB to a high-fat diet in mice increased fecal lipid content, indicating reduced absorption of lipids as the mechanism underlying antiobesity effect. The investigation of bioactive compounds in YB resulted in the identification of fructose–bisphosphate aldolase as a proteinous lipase inhibitor. Maximum inhibition of the protein was 45%, but inhibition was displayed at a concentration as low as 16 ng/mL, which is a characteristic inhibition compared with other reported proteinous lipase inhibitors.

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Megawati, Megawati, Nina Artanti, Hani Mulyani, Akhmad Darmawan, Heri Syahrian, Puspa Dewi N. Lotulung, Edi Supriadi, et al. "In vitro lipase enzyme inhibitory activities of green tea and other herbs." Jurnal Gizi Indonesia (The Indonesian Journal of Nutrition) 9, no. 1 (December 18, 2020): 48–52. http://dx.doi.org/10.14710/jgi.9.1.48-52.

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Background: Increased lipase activity can increase the amount of monoglycerides and fatty acids absorbed by the body, this is what affects obesity. If pancreatic lipase activity is inhibited, the production of fatty acids will decrease, consequently the level of fat in the blood will also decrease.Objective: To study anti obesity potential of a single herb or a mixture of green tea and other herbs (Syzygium polyanthum. Lv, Artocarpus communis.Lv, Cinnamomum verum..Lv, Manilkara zapota.Lv, Tectona grandis.Lv) by the in vitro inhibition assay of the lipase enzyme activityMethod: A single (8 herbs) or a mixture of three herbs powder (12 formulas) was put into a tea bag with a total weight of 1.5 g to be brewed in 100 mL bottled mineral water at 70⁰-90⁰C for 10 minutes. In vitro lipase enzyme inhibition assay were conducted to measure the ability of these samples as lipase inhibitor. Orlistat used as positive lipase inhibitor. Results: There was a difference results of lipase inhibition activity between the sample of a single and a mixture of herbs. Interestingly, the results shows that formula 3 (mixture of green tea, Manilkara zapota and cinnamon). has 53.942 % inhibition, formula 9 (a mixture of green tea, Syzygium polyanthum and cinnamon) has 67.322 % inhibition and formula 12 (a mixture of green tea, Tectona grandis and cinnamon) has 56.612 % inhibition which close to lipase inhibitory activity by standard Orlistat.Conclusion: The mixture of green tea and two other herbs has a lipase inhibitory activity similar to Orlistat, when compared to the single herb. The highest lipase inhibitory activity is found in formula 9.

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Fex, Malin, and Hindrik Mulder. "Lipases in the pancreatic β-cell: implications for insulin secretion." Biochemical Society Transactions 36, no. 5 (September 19, 2008): 885–90. http://dx.doi.org/10.1042/bst0360885.

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Lipids have been implicated in β-cell stimulus–secretion coupling. In such a role, lipases in β-cells would be required to generate lipid coupling factors. We have shown previously that glucose stimulates lipolysis in rodent islets. In addition, lipolysis and diacylglycerol lipase activity in islets are abolished by orlistat, an irreversible lipase inhibitor with a broad specificity for substrates. Moreover, orlistat dose-dependently inhibits glucose- and forskolin-stimulated insulin secretion, while leaving glucose oxidation and the rise in the ATP/ADP ratio intact. In an effort to identify β-cell lipase(s), we found that HSL (hormone-sensitive lipase), the rate-limiting enzyme for acylglycerol hydrolysis in adipocytes, is expressed in rodent β-cells. To resolve the role of this lipase, we have created global and β-cell-specific knockout mice. Although our line of global HSL-knockout mice is moderately glucose-intolerant owing to reduced peripheral insulin sensitivity and exhibits normal islet metabolism and insulin secretion, other HSL-knockout lines have displayed impaired insulin secretion under certain conditions. In contrast, β-cell-specific HSL-knockout mice, which are less prone to genetic redundancy, are hyperglycaemic, presumably caused by a perturbation of first-phase insulin secretion. Thus studies by us and others demonstrate that lipases, such as HSL, play a regulatory role in β-cell stimulus–secretion coupling.

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Chakraborty, Sandeep, Adela Rendón-Ramírez, Bjarni Ásgeirsson, Mouparna Dutta, Anindya S. Ghosh, Masataka Oda, Ravindra Venkatramani, Basuthkar J. Rao, Abhaya M. Dandekar, and Félix M. Goñi. "Dipeptidyl peptidase-IV inhibitors used in type-2 diabetes inhibit a phospholipase C: a case of promiscuous scaffolds in proteins." F1000Research 2 (January 14, 2015): 286. http://dx.doi.org/10.12688/f1000research.2-286.v2.

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The long term side effects of any newly introduced drug is a subject of intense research, and often raging controversies. One such example is the dipeptidyl peptidase-IV (DPP4) inhibitor used for treating type 2 diabetes, which is inconclusively implicated in increased susceptibility to acute pancreatitis. Previously, based on a computational analysis of the spatial and electrostatic properties of active site residues, we have demonstrated that phosphoinositide-specific phospholipase C (PI-PLC) from Bacillus cereus is a prolyl peptidase using in vivo experiments. In the current work, we first report the inhibition of the native activity of PI-PLC by two DPP4 inhibitors - vildagliptin (LAF-237) and K-579. While vildagliptin inhibited PI-PLC at micromolar concentrations, K-579 was a potent inhibitor even at nanomolar concentrations. Subsequently, we queried a comprehensive, non-redundant set of 5000 human proteins (50% similarity cutoff) with known structures using serine protease (SPASE) motifs derived from trypsin and DPP4. A pancreatic lipase and a gastric lipase are among the proteins that are identified as proteins having promiscuous SPASE scaffolds that could interact with DPP4 inhibitors. The presence of such scaffolds in human lipases is expected since they share the same catalytic mechanism with PI-PLC. However our methodology also detects other proteins, often with a completely different enzymatic mechanism, that have significantly congruent domains with the SPASE motifs. The reported elevated levels of serum lipase, although contested, could be rationalized by inhibition of lipases reported here. In an effort to further our understanding of the spatial and electrostatic basis of DPP4 inhibitors, we have also done a comprehensive analysis of all 76 known DPP4 structures liganded to inhibitors till date. Also, the methodology presented here can be easily adopted for other drugs, and provide the first line of filtering in the identification of pathways that might be inadvertently affected due to promiscuous scaffolds in proteins.

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Chakraborty, Sandeep, Adela Rendón-Ramírez, Bjarni Ásgeirsson, Mouparna Dutta, Anindya S. Ghosh, Masataka Oda, Ravindra Venkatramani, Basuthkar J. Rao, Abhaya M. Dandekar, and Félix M. Goñi. "The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins." F1000Research 2 (January 29, 2015): 286. http://dx.doi.org/10.12688/f1000research.2-286.v3.

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The long term side effects of any newly introduced drug is a subject of intense research, and often raging controversies. One such example is the dipeptidyl peptidase-IV (DPP4) inhibitor used for treating type 2 diabetes, which is inconclusively implicated in increased susceptibility to acute pancreatitis. Previously, based on a computational analysis of the spatial and electrostatic properties of active site residues, we have demonstrated that phosphoinositide-specific phospholipase C (PI-PLC) from Bacillus cereus is a prolyl peptidase using in vivo experiments. In the current work, we first report the inhibition of the native activity of PI-PLC by two DPP4 inhibitors - vildagliptin (LAF-237) and K-579. While vildagliptin inhibited PI-PLC at micromolar concentrations, K-579 was a potent inhibitor even at nanomolar concentrations. Subsequently, we queried a comprehensive, non-redundant set of 5000 human proteins (50% similarity cutoff) with known structures using serine protease (SPASE) motifs derived from trypsin and DPP4. A pancreatic lipase and a gastric lipase are among the proteins that are identified as proteins having promiscuous SPASE scaffolds that could interact with DPP4 inhibitors. The presence of such scaffolds in human lipases is expected since they share the same catalytic mechanism with PI-PLC. However our methodology also detects other proteins, often with a completely different enzymatic mechanism, that have significantly congruent domains with the SPASE motifs. The reported elevated levels of serum lipase, although contested, could be rationalized by inhibition of lipases reported here. In an effort to further our understanding of the spatial and electrostatic basis of DPP4 inhibitors, we have also done a comprehensive analysis of all 76 known DPP4 structures liganded to inhibitors till date. Also, the methodology presented here can be easily adopted for other drugs, and provide the first line of filtering in the identification of pathways that might be inadvertently affected due to promiscuous scaffolds in proteins.

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Chakraborty, Sandeep, Adela Rendón-Ramírez, Bjarni Ásgeirsson, Mouparna Dutta, Anindya S. Ghosh, Masataka Oda, Ravindra Venkatramani, Basuthkar J. Rao, Abhaya M. Dandekar, and Félix M. Goñi. "Dipeptidyl peptidase-IV inhibitors used in type-2 diabetes inhibit a phospholipase C: a case of promiscuous scaffolds in proteins." F1000Research 2 (December 27, 2013): 286. http://dx.doi.org/10.12688/f1000research.2-286.v1.

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The long term side effects of any newly introduced drug is a subject of intense research, and often raging controversies. One such example is the dipeptidyl peptidase-IV (DPP4) inhibitor used for treating type 2 diabetes, which is inconclusively implicated in increased susceptibility to acute pancreatitis. Previously, based on a computational analysis of the spatial and electrostatic properties of active site residues, we have demonstrated that phosphoinositide-specific phospholipase C (PI-PLC) from Bacillus cereus is a prolyl peptidase using in vivo experiments. In the current work, we first report the inhibition of the native activity of PI-PLC by two DPP4 inhibitors - vildagliptin (LAF-237) and K-579. While vildagliptin inhibited PI-PLC at micromolar concentrations, K-579 was a potent inhibitor even at nanomolar concentrations. Subsequently, we queried a comprehensive, non-redundant set of 5000 human proteins (50% similarity cutoff) with known structures using serine protease (SPASE) motifs derived from trypsin and DPP4. A pancreatic lipase and a gastric lipase are among the proteins that are identified as proteins having promiscuous SPASE scaffolds that could interact with DPP4 inhibitors. The presence of such scaffolds in human lipases is expected since they share the same catalytic mechanism with PI-PLC. However our methodology also detects other proteins, often with a completely different enzymatic mechanism, that have significantly congruent domains with the SPASE motifs. The reported elevated levels of serum lipase, although contested, could be rationalized by inhibition of lipases reported here. Also, the methodology presented here can be easily adopted for other drugs, and provide the first line of filtering in the identification of pathways that might be inadvertently affected due to promiscuous scaffolds in proteins.

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Kim, Min Young. "INHIBITORY ACTIVITIES OF CAMELLIA MISTLETOE (K. JAPONICA) EXTRACTS ON PANCREATIC LIPASE, TYROSINASE AND CANCER CELL PROLIFERATION." International Journal of Pharmacy and Pharmaceutical Sciences 9, no. 10 (October 2, 2017): 187. http://dx.doi.org/10.22159/ijpps.2017v9i10.21304.

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Objective: The objective of this study was undertaken to examine pancreatic lipase and tyrosinase inhibitory activities of Camellia mistletoe (Korthalsella japonica) extracts and conduct their antiproliferative activity on several human cancer (Hela, A375, HCT 116, HepG2 and A549) and normal cells (TK6) lines.Methods: The lipase inhibitory activity of acts of Camellia mistletoe extracts were determined from the hydrolytic reaction of p-nitrophenyl butyrate with pancreatic lipase and cytotoxicity against human cancer and normal cell lines were also evaluated using the MTT assay. The in vitro tyrosinase inhibitor potency of Camellia mistletoe extracts was estimated using mushroom tyrosinase.Results: Both methanol and ethanol extracts of Camellia mistletoe exhibited an inhibitory effect on lipase inhibition activity with IC50 values of 0.39 and 0.49 mg/ml, respectively. Moreover, Camellia mistletoe extracts were judged to be strongly active against the cancer cell lines, while they had no antiproliferative activity against the normal human cell lines. However, they had little inhibitory effects on tyrosinase activity.Conclusion: Camellia mistletoe extracts could be the good sources of natural lipase inhibition and anticancer agents with a great potential to be used in food and therapeutic fields.

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Patil, Mohini, Ravindra Patil, Bhushan Bhadane, Shahid Mohammad, and Vijay Maheshwari. "Pancreatic lipase inhibitory activity of phenolic inhibitor from endophytic Diaporthe arengae." Biocatalysis and Agricultural Biotechnology 10 (April 2017): 234–38. http://dx.doi.org/10.1016/j.bcab.2017.03.013.

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Hamdan, Imad I., Violet N. Kasabri, Yusuf M. Al-Hiari, Dina El-Sabawi, and Hiba Zalloum. "Pancreatic lipase inhibitory activity of selected pharmaceutical agents." Acta Pharmaceutica 69, no. 1 (March 1, 2019): 1–16. http://dx.doi.org/10.2478/acph-2019-0010.

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Abstract Twenty-five structurally diverse compounds have been tested in vitro for their pancreatic lipase (PL) inhibitory activity. Despite the diversity of tested compounds, the relationship comprising structural attributes of the compounds could be established to correlate with the observed inhibitory activity. Compounds that exerted inhibitory action through surface activity were of different profile from the rest of compounds. When co-incubated with orlistat (OsT), important synergistic effects for some compounds (orphenadrine, gliclazide, cefuroxime and sulfacetamide) were revealed, while antagonistic effects were demonstrated for others (camphor sulfonic acid and dinitro salicylic acid). Docking studies for the most active molecules were performed and molecular interaction forces with the PL active site were identified. The results suggested co-binding of OsT along with the other inhibitor in the binding site in cases of synergistic effect but not in the case of antagonistic effect. These results were additionally supported by affinity capillary electrophoresis. In conclusion, synergistic lipase inhibitory activity between OsT and some other pharmaceutical compounds was demonstrated for the first time, which might help improve the pharmacological effect of OsT.

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Ahn, Jong Hoon, Qing Liu, Chul Lee, Mi-Jeong Ahn, Hwan-Soo Yoo, Bang Yeon Hwang, and Mi Kyeong Lee. "A new pancreatic lipase inhibitor from Broussonetia kanzinoki." Bioorganic & Medicinal Chemistry Letters 22, no. 8 (April 2012): 2760–63. http://dx.doi.org/10.1016/j.bmcl.2012.02.088.

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Shawky, Suzan, Ali A. Ali, and Mohammed Abdalla Hussein. "Green Synthesis of SP-SeNPs as Promising Antioxidant Agent and Pancreatic Lipase Inhibitor." Asian Journal of Chemistry 34, no. 7 (2022): 1729–34. http://dx.doi.org/10.14233/ajchem.2022.23608.

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The purpose of this study was to evaluate pancreatic lipase inhibitory activity and antioxidant effect of Spirulina platensis containing selenium nanoemulsion nanoparticles (SP-SeNPs). The SP-SeNPs were prepared and characterized to find mean particle size and zeta potential to evaluate the possible lipoprotein lipase and pancreatic lipase inhibitory as well as antioxidant and free radical scavenging activities. Different antioxidant tests were employed, namely, reducing power, chelating activity on Fe2+, free radical-scavenging and total antioxidant activities. The obtained results showed that the shapes of SP-SeNPs were spherical and the mean particle size was 39.86 ± 0.14 nm and negative zeta potential was +33.14. The SP-SeNP at 60 ppm and epicatechin (100 ppm) produce the same ratio of inhibition 18%. However, lipoprotein lipase activity was increased to less than 20 and 27 % at 80 and 100 ppm SP-SeNPs. Also, the present results indicate that the SP-SeNPs at concentration of 80 and 100 ppm showed inhibitory effects more than epicatechin (100 ppm) against pancreatic lipase activity. However, the reducing power of SP-SeNPs and butylated hydroxytoluene (BHT), butylated hydroxy anisole (BHA) and α-tocopherol decreased in the order of BHA> SP-SeNPs >BHT > α-tocopherol. The chelating activity of samples increased with increasing incubation times with FeCl2. However, the chelating activity of SP-SeNPs of 1.50 mg/mL was nearly equal to EDTA at 0.037 mg/mL (43.67%) for an incubation time of 60 min. This indicates that the chelation property of the samples on Fe2+ ions may afford protection against oxidative damage. The SP-SeNPs of 6 mg/mL had the highest radical scavenging activity when compared with 0.6 mg/mL Trolox. The antioxidant activity of SP-SeNPs and both standards decreased in the order of SP-SeNPs > α-tocopherol > Trolox > BHA > BHT. The results suggested that the inhibitory activity of SP-SeNPs is closely related to the tertiary structural change in lipoprotein lipase and pancreatic lipase. Also, the antioxidant activity of SP-SeNPs could be due to presence of carotenoids, ω-3 or ω-6 polyunsaturated fatty acid, γ-linolenic acid, sulpholipides, glycolipids, potassium, zinc and selenium, vitamin A, vitamin E and a variety of minerals.

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Muhd Rodhi, Miradatul Najwa, Ku Halim Ku Hamid, Fazlena Hamzah, Nur Syafiqah Kamarul Bahari, and Nur Amira Abdul Rahman. "Inhibition of pancreatic lipase by gallic acid and quercetin equivalent in ultrasonicated Malaysian grown Aquilaria spp. leaves of different particle size." Malaysian Journal of Chemical Engineering and Technology (MJCET) 3, no. 2 (December 31, 2020): 1. http://dx.doi.org/10.24191/mjcet.v3i2.10942.

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Pancreatic lipase inhibitory compounds (gallic acid and quercetin) and their inhibition properties were determined in the crude extract of matured leaves from widely grown Aquilaria spp. in Malaysia, which are Aquilaria malaccensis and Aquilaria subintegra. The leaves were dried at 60 °C for 24 hours and undergone a pre-treatment method by using ultrasonication, within 30 minutes of reaction. Dried matured leaves were ground and sieved into particle sizes of 250, 300, 400, 500, and 1000 µm. Each particle size was soaked in distilled water with a ratio of 1% (w/v) for 24 hours, prior to ultrasonication process. Particle size of 250 µm resulted in the highest concentration of gallic acid and quercetin equivalent for both species of Aquilaria, wherein 89.99 mg/ml of gallic acid equivalent and 0.0295 mg/ml of quercetin equivalent were obtained in A. malaccensis crude leaves extract and in A. subintegra crude extract, 101.27 mg/ml and 0.0373 mg/ml were obtained, respectively. Thus, this sample was used in the inhibition study of pancreatic lipase. The concentrations of substrate and enzyme activity prepared were varied in the inhibition kinetics study. Based on the inhibition of pancreatic lipase, the crude leaves extract of both Aquilaria species exhibited the mixed-inhibition which is also known to be the non-competitive inhibition because the reaction mechanism showing the binding of inhibitor to the free pancreatic lipase and pancreatic lipase-substrate complex. This research is one of the fundamental works for future studies on the natural source to control obesity, which is a new direction of the key research in lipase inhibition.

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Amereih, Sameer, Abd Daraghmeh, Ismail Warad, and Mohammed Al-Nuri. "Synthesis and Evaluation of Anti-Lipase Potential and Molecular Docking of N’-(2-Hydroxy-5-nitrobenzylidene) naphthalene-2-sulfonohydrazide." مجلة جامعة فلسطين التقنية للأبحاث 8, no. 2 (September 1, 2020): 01–11. http://dx.doi.org/10.53671/pturj.v8i2.17.

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N’-(2-Hydroxy-5-nitrobenzylidene) naphthalene-2-sulfonohydrazide (SB) was prepared by condensation reaction, of naphthalene-2-sulfonylchloride with 2-Hydroxy-5-nitrobenzaldehyde. The Schiff base product (SB) was isolated, purified and then spectrally characterized via UV-Vis, FT-IR, 1H and 13C NMR analysis, where strong evidences confirmed the formation of the desired product. Pancreatic porcine lipase inhibition of the Schiff base product was evaluated and compared with the reference “Orlistat”. The product was an active as a lipase enzyme inhibitor with IC50 42.65±0.97 mcg/ml. The molecular docking of the compound with porcine pancreatic lipase was investigating, the results of theoretical docking explained the experimental one since several hydrogen bonds between the Schiff base compound and amino acids in lipase were detected. Antimicrobial activity of SB product was also evaluated in vitro against several types of bacteria such as: Escherichia coli, Staphylococcus aureus, Pseudomonas aeruginosa, Klebsiella pneumonia and MRSA by Minimum Inhibitory Concentration (MIC) test using tetracycline (TE) as a standard antibiotic. Results showed a bacteriostatic effect of this compound against bacteria such as MRSA, P. aeruginosa and K. pneumoniae

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Amereih, Sameer, Abd Daraghmeh, Ismail Warad, and Mohammed Al-Nuri. "Synthesis and Evaluation of Anti-Lipase Potential and Molecular Docking of N’-(2-Hydroxy-5-nitrobenzylidene) naphthalene-2-sulfonohydrazide." مجلة جامعة فلسطين التقنية خضوري للأبحاث 8, no. 2 (September 1, 2020): 01–11. http://dx.doi.org/10.53671/ptukrj.v8i2.17.

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N’-(2-Hydroxy-5-nitrobenzylidene) naphthalene-2-sulfonohydrazide (SB) was prepared by condensation reaction, of naphthalene-2-sulfonylchloride with 2-Hydroxy-5-nitrobenzaldehyde. The Schiff base product (SB) was isolated, purified and then spectrally characterized via UV-Vis, FT-IR, 1H and 13C NMR analysis, where strong evidences confirmed the formation of the desired product. Pancreatic porcine lipase inhibition of the Schiff base product was evaluated and compared with the reference “Orlistat”. The product was an active as a lipase enzyme inhibitor with IC50 42.65±0.97 mcg/ml. The molecular docking of the compound with porcine pancreatic lipase was investigating, the results of theoretical docking explained the experimental one since several hydrogen bonds between the Schiff base compound and amino acids in lipase were detected. Antimicrobial activity of SB product was also evaluated in vitro against several types of bacteria such as: Escherichia coli, Staphylococcus aureus, Pseudomonas aeruginosa, Klebsiella pneumonia and MRSA by Minimum Inhibitory Concentration (MIC) test using tetracycline (TE) as a standard antibiotic. Results showed a bacteriostatic effect of this compound against bacteria such as MRSA, P. aeruginosa and K. pneumoniae

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Borges, Josileide Gonçalves, Jackson Roberto Guedes da Silva Almeida, Juliana Anielle Ribeiro De Sá, Kaline Stela Pires Bezerra, Patricia Kauanna Fonseca Damasceno, Isabela Mary Alves Reis, and Marigilson Pontes De Siqueira Moura. "Inhibition of Pancreatic Lipase and Characterization by Extracts From Fruit Pomaces Cultivars Grown in Brazilian Semiarid." Journal of Agricultural Studies 7, no. 2 (November 10, 2019): 343. http://dx.doi.org/10.5296/jas.v7i4.15410.

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Investigate action of pancreatic lipase inhibition and characterization of extracts obtained from fruit pomace cultivars grown in Brazilian semiarid. Phytochemicals of Vitis labrusca, Passiflora edulis flavicarpa Deg., Citrus sinensis L Osbeck, and Punica granatum L. were extracted by maceration in a hydroethanolic solution. Inhibition activity of pancreatic lipase was performed by ELISA reader. To identify which compounds would probably be responsible for inhibitory activity, extracts were characterized by method of total phenolics using folin ciocalteau, phenolic acids and flavonoids were identified by HPLC, antioxidant potential was quantified by DPPH. With exception of pomegranate seed, all other pomace showed potential for inhibition of lipase. However, V. labrusca had higher percentage of inhibition (89.74%), this percentage similar to that obtained by commercial orlistat inhibitor, which would indicate its use as an efficient inhibitor. For all extracts were found several phytochemical compounds with phenolic characteristics, however, pomaces of P. granatum peel and V. labrusca showed best results in total phenolic and antioxidant activity. P. granatum peel had a high content of total phenolics (82.50 EAG g-1) and the best antioxidant activity (IC50 = 1.47 µg mL-1). All pomace extracts showed varied secondary metabolites, although antioxidant activity from grape and passion fruit pomaces showed potential for inhibition of lipids absorption.

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Panwar, Umesh, and Sanjeev Kumar Singh. "Identification of Novel Pancreatic Lipase Inhibitors Using In Silico Studies." Endocrine, Metabolic & Immune Disorders - Drug Targets 19, no. 4 (June 12, 2019): 449–57. http://dx.doi.org/10.2174/1871530319666181128100903.

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Background: Obesity is well known multifactorial disorder towards the public health concern in front of the world. Increasing rates of obesity are characterized by liver diseases, chronic diseases, diabetes mellitus, hypertension and stroke, improper function of the heart, reproductive and gastrointestinal diseases, and gallstones. An essential enzyme pancreatic lipase recognized for the digestion and absorption of lipids can be a promising drug target towards the future development of antiobesity therapeutics in the cure of obesity disorders. Objective: The purpose of present study is to identify an effective potential therapeutic agent for the inhibition of pancreatic lipase. Methods: A trio of in-silico procedure of HTVS, SP and XP in Glide module, Schrodinger with default parameters, was applied on Specs databases to identify the best potential compound based on receptor grid. Finally, based on binding interaction, docking score and glide energy, selected compounds were taken forward to the platform of IFD, ADME, MMGBSA, DFT, and MDS for analyzing the ligands behavior into the protein binding site. Results: Using in silico protocol of structure-based virtual screening on pancreatic lipase top two compounds AN-465/43369242 & AN-465/43384139 from Specs database were reported. The result suggested that both the compounds are competitive inhibitors with higher docking score and greatest binding affinity than the reported inhibitor. Conclusion: We anticipate that results could be future therapeutic agents and may present an idea toward the experimental studies against the inhibition of pancreatic lipase.

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Meyer, J. H., J. D. Elashoff, M. Domeck, A. Levy, D. Jehn, M. Hlinka, R. Lake, L. S. Graham, and Y. G. Gu. "Control of canine gastric emptying of fat by lipolytic products." American Journal of Physiology-Gastrointestinal and Liver Physiology 266, no. 6 (June 1, 1994): G1017—G1035. http://dx.doi.org/10.1152/ajpgi.1994.266.6.g1017.

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Dietary fat is ingested in three forms: 1) in solid food, 2) as aqueous emulsions, and 3) as unemulsified, liquid oil. On the basis of a scant previous literature, we postulated that liquid fat (emulsions or oils) would empty from the stomach at speeds that varied with the amounts ingested but that this dynamic would be modulated by feedback inhibition from lipolytic products. To test these ideas, we used a gamma camera to track gastric emptying of 123I-labeled fat in dogs with chronic pancreatic fistulas by which lipase was excluded from or replenished in the duodenum in varied amounts after dogs were fed 15-, 30-, and 60-g loads of liquid fat given with solid foods or as emulsions. We also tracked concurrent gastric emptying of 113mIn, which marked the solid food phase or the water phase of emulsions. In some studies, we used a potent and specific inhibitor (orlistat) of pancreatic and gastric lipases to assess how lipolytic products modulated emptying of liquid fat. In the absence of pancreatic enzymes, both oils and emulsions emptied initially at high speeds that varied with fat loads, but emptying slowed 20 min after ingestion of emulsions and 60 min after ingestion of unemulsified oil. Studies with orlistat indicated that these changes in rates resulted from liberation of gastric lipolytic products. Emptying of oil emulsions was not altered by duodenal replenishment with pancreatic enzymes, but emptying of unemulsified oil was inhibited in a dose-related fashion, such that maximal inhibition was achieved when pancreatic enzymes were replenished at > or = 40% of normal amounts. Studies with orlistat confirmed that this dose-dependent slowing was due specifically to lipase. Emptying of solid food was much more sensitive to replenishment with enzymes, so that a 10% replenishment maximally inhibited solid emptying.

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STAMATIS, HARALAMBOS, DIMITRIOS GOURNIS, ANGELIKI POLYDERA, STAMATIA SPYROU, KONSTANTINOS SPYROU, ELENA GKANTZOU, and ANASTASIA SKONTA. "3D Printed Polylactic Acid (PLA) Well Plates for Enzyme Inhibition Studies: The Case of Pancreatic Lipase." Catalysis Research 02, no. 04 (October 8, 2022): 1–19. http://dx.doi.org/10.21926/cr.2203032.

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3D printed PLA has already been demonstrated for several biotechnological applications, including enzymes immobilization. The prerequisites for an efficient screening assay include using small volumes of reagents, low cost, and rapid screening of large numbers of compounds and extracts. Hence, assays based on microtiter plates are predominant. Thus, designing and fabricating scaffolds on a similar scale, which could serve as immobilization carriers, and their recruitment in inhibitors screening studies is of great significance, adding both enzyme stability and reuse potentiality of the biocatalytic system in assay merits. In this work, pancreatic lipase was immobilized on 3D-printed PLA microwells for enzyme inhibitor screening. XPS analysis demonstrated the successful modification of the PLA scaffolds. The immobilized enzyme displayed high levels of operational, thermal, and storage stability under the tested conditions. The IC<sub>50</sub> values for PPL inhibition were calculated for Orlistat, a model lipase inhibitor, and olive leaf extract, a promising natural compound. This is the first study reporting the use of 3D-printed PLA wells with an immobilized enzyme for inhibitor screening assay.

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Marrelli, Mariangela, Federica Morrone, Maria Argentieri, Lucia Gambacorta, Filomena Conforti, and Pinarosa Avato. "Phytochemical and Biological Profile of Moricandia arvensis (L.) DC.: An Inhibitor of Pancreatic Lipase." Molecules 23, no. 11 (October 31, 2018): 2829. http://dx.doi.org/10.3390/molecules23112829.

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Pancreatic lipase, a key enzyme for lipid absorption, is one of the most important targets for the treatment of obesity, while natural compounds have recently attracted much interest as potential inhibitors of this enzyme. Here, in an attempt to find new effective agents, the methanolic extract from Moricandia arvensis (L.) DC. and its sub-extracts were investigated for their potential inhibitory activity. The ability to inhibit pancreatic lipase was verified through the in vitro evaluation of the prevention of p-nitrophenyl caprylate hydrolysis. The antioxidant activity was also verified by means of DPPH and β-carotene bleaching tests. Compositional profiling revealed that flavonoid glycosides were the main specialized metabolites present in the methanolic extract from the aerial parts of the plant with kaempferol and quercetin representing the two O-glycosylated aglycones. Kaempferol-3-O-β-(2″-O-glucosyl)-rutinoside and kaempferol-3-O-a-arabinosyl-7-O-rhamnoside were the most abundant flavonols. The crude methanolic extract and the dichloromethane and ethyl acetate sub-extracts showed a strong lipase inhibitory activity, with IC50 values of 2.06 ± 0.02, 1.52 ± 0.02 and 1.31 ± 0.02 mg/mL, respectively. The best capacity to scavenge DPPH radical was detected for the ethyl acetate sub-extract (IC50 = 171.9 ± 1.0 µg/mL), which was also effective in protecting linoleic acid from peroxidation (IC50 = 35.69 ± 2.30 µg/mL). Obtained results support the hypothesis that M. arvensis can be a source of bioactive phytochemicals for the pharmacological inhibition of dietary lipids absorption.

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Oliveira, Luana Carvalho de, Danielle Lima Bezerra de Menezes, Valéria Costa da Silva, Estela Mariana Guimarães Lourenço, Paulo Henrique Santana Miranda, Márcia de Jesus Amazonas da Silva, Emerson Silva Lima, et al. "In Silico Study, Physicochemical, and In Vitro Lipase Inhibitory Activity of α,β-Amyrenone Inclusion Complexes with Cyclodextrins." International Journal of Molecular Sciences 22, no. 18 (September 13, 2021): 9882. http://dx.doi.org/10.3390/ijms22189882.

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α,β-amyrenone (ABAME) is a triterpene derivative with many biological activities; however, its potential pharmacological use is hindered by its low solubility in water. In this context, the present work aimed to develop inclusion complexes (ICs) of ABAME with γ- and β-cyclodextrins (CD), which were systematically characterized through molecular modeling studies as well as FTIR, XRD, DSC, TGA, and SEM analyses. In vitro analyses of lipase activity were performed to evaluate possible anti-obesity properties. Molecular modeling studies indicated that the CD:ABAME ICs prepared at a 2:1 molar ratio would be more stable to the complexation process than those prepared at a 1:1 molar ratio. The physicochemical characterization showed strong evidence that corroborates with the in silico results, and the formation of ICs with CD was capable of inducing changes in ABAME physicochemical properties. ICs was shown to be a stronger inhibitor of lipase activity than Orlistat and to potentiate the inhibitory effects of ABAME on porcine pancreatic enzymes. In conclusion, a new pharmaceutical preparation with potentially improved physicochemical characteristics and inhibitory activity toward lipases was developed in this study, which could prove to be a promising ingredient for future formulations.

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YOUNG, Simon C., and David Y. HUI. "Pancreatic lipase/colipase-mediated triacylglycerol hydrolysis is required for cholesterol transport from lipid emulsions to intestinal cells." Biochemical Journal 339, no. 3 (April 26, 1999): 615–20. http://dx.doi.org/10.1042/bj3390615.

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This study tested the hypothesis that dietary cholesterol uptake by intestinal cells is dependent on the structure and composition of the lipid carriers in the extracellular milieu. In in vivo experiments with female C57BL/6 mice, cholesterol absorption from phospholipid/triacylglycerol emulsions was significantly reduced by administration of tetrahydrolipstatin, an inhibitor of pancreatic lipase. This inhibitor had no effect on the absorption of cholesterol from phospholipid vesicles. The importance of pancreatic-lipase-mediated triacylglycerol hydrolysis for cholesterol transport from emulsions to intestinal cells was confirmed by in vitro experiments with rat IEC-6 intestinal cells. Cellular uptake of cholesterol from emulsions with a phospholipid/triacylglycerol molar ratio of < 0.3 could be stimulated by pancreatic lipase/colipase hydrolysis of the core neutral lipids. However, pancreatic lipase/colipase was ineffective in hydrolysing triacylglycerols in emulsions with a phospholipid/triacylglycerol molar ratio of > 0.3. Phospholipase A2-mediated hydrolysis of the surface phospholipids was necessary prior to triacylglycerol hydrolysis in these phospholipid-rich emulsions and to the stimulation of cholesterol transport from these particles to IEC-6 cells. The data also revealed that minimal triacylglycerol hydrolysis was sufficient to significantly increase cholesterol transport from lipid emulsions to the intestinal cells. Thus the products of triacylglycerol hydrolysis, namely monoacylglycerol and non-esterified fatty acids, are key determinants in mediating cholesterol transport from lipid emulsions to intestinal cells. Taken together, these results support the hypothesis that remodelling of the surface and core components of lipid carriers is necessary prior to absorption of dietary cholesterol from the gastrointestinal tract.

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Karu, Naama, Ram Reifen, and Zohar Kerem. "Weight Gain Reduction in Mice FedPanaxginsengSaponin, a Pancreatic Lipase Inhibitor." Journal of Agricultural and Food Chemistry 55, no. 8 (April 2007): 2824–28. http://dx.doi.org/10.1021/jf0628025.

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Ahn, Jong Hoon, Qing Liu, Chul Lee, Mi-Jeong Ahn, Hwan-Soo Yoo, Bang Yeon Hwang, and Mi Kyeong Lee. "ChemInform Abstract: A New Pancreatic Lipase Inhibitor from Broussonetia kanzinoki." ChemInform 43, no. 35 (August 2, 2012): no. http://dx.doi.org/10.1002/chin.201235220.

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Faridah, Faridah, Wahono Sumaryono, Partomuan Simanjuntak, and Rizki Riyadi Triwibowo. "Analysis of Pancreatic Lipase Inhibitor Activity of Chlorogenic Acid Derivatives in Green Coffee Beans as Antiobesity using In Silico." JURNAL ILMU KEFARMASIAN INDONESIA 19, no. 1 (April 30, 2021): 125. http://dx.doi.org/10.35814/jifi.v19i1.946.

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Obesity or overweight is defi ned as the accumulation of abnormal or excessive fat in adipose tissue whichcan damage health.Several plants have been used empirically as antiobesity.This study aims to obtain candidate antiobesity compounds that act as pancreatic lipase enzyme inhibitors, fi nd some amino acids that involved on the active site of the receptors and modelling the interactions of these active compounds at antiobesity receptors.The study start with internal validation of the receptors used (4DOQ), then carried out the docking process for the native ligand, comparison compound (Orlistat) and each test compound with the same receptor. The softwares used are PLANTS, YASARA, ChemSketch, and Pymol. The results of the 4DOQ receptor validation have an RMSD value of 1.7097 Ǻ. The results of the docking score for orlistat (-65.3258), and 4 active compounds namely chlorogenic acid (-69,3009), 5-O-caff eoylquinat acid (-70.6911), 4,5-O-dicaff eoilkuinic acid (-85 , 3375), 5-Op-coumaroilkuinic acid (-67,1886). Amino acids that play a role in the affi nity on the active side of the ligand bond with the pancreatic lipase receptor are THR21 (Threonine), ASN84 (Asparagine), GLY19 (Glycine), GLN156 (Glutamine), ALA85 (Alanine), ILE63 (Isoleucine), ARG62 (Arginine) . The conclusion of this study there are 4 chemical compounds in green coff ee beans that are active as antiobesity with the mechanism of action of the pancreatic lipase enzyme inhibitor, namely chlorogenic acid, 5-O-caff eoylquinic acid, 4,5-O-diphoeilquinic acid, 5-op-coumaroilquinic acid.

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Liu, Tian-Tian, Xiao-Tian Liu, Gui-Li Huang, Long Liu, Qing-Xi Chen, and Qin Wang. "Theophylline Extracted from Fu Brick Tea Affects the Metabolism of Preadipocytes and Body Fat in Mice as a Pancreatic Lipase Inhibitor." International Journal of Molecular Sciences 23, no. 5 (February 25, 2022): 2525. http://dx.doi.org/10.3390/ijms23052525.

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The dramatic increase in obesity is putting people under increasing pressure. Lipase inhibitors, as a kind of effective anti-obesity drug, have attracted more and more researchers’ attention in recent years because of their advantages of acting on the intestinal tract and having no side effects on the central nervous system. In this study, lipase inhibitor Fu Brick Theophylline (FBT) was screened based on enzyme molecular dynamics, and the inhibition mechanism of lipase inhibitors on obesity was analyzed and discussed at the cellular level and animal model level. We found that FBT had high inhibition effects of lipase with an IC50 of 1.02~0.03 μg/mL. Firstly, the laboratory used 3T3-L1 proadipocytes as models, flow cytometry was used to detect the effects of FBT on the cycle, apoptosis and intracellular ROS activity of proadipocytes. To study the contents of triglyceride, total cholesterol, related metabolites and related gene and protein expression in adipocytes. The results showed that FBT could reduce ROS production and inflammatory factor mRNA expression during cell differentiation. Secondly, by establishing the animal model of high-fat feed ob nutritional obese mice, the morphological observation and gene expression analysis of body weight, fat rate, adipocyte and hepatocyte metabolism of FBT obese mice were further discussed. It was proven that FBT can effectively reduce the degree of fatty liver, prevent liver fibrosis and fat accumulation, and improve the damage of mitochondrial membrane structure. This study provides a theoretical basis for the screening and clinical treatment of lipase inhibitors.

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Fadillah, Wendi Nurul, Nampiah Sukarno, Dyah Iswantini, Min Rahminiwati, Novriyandi Hanif, and Mashuri Waite. "In Vitro Pancreatic Lipase Inhibition by Marine Fungi Purpureocillium lilacinum Associated with Stylissa sp. Sponge as Anti-obesity Agent." HAYATI Journal of Biosciences 29, no. 1 (December 9, 2021): 76–86. http://dx.doi.org/10.4308/hjb.29.1.76-86.

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This study aimed to evaluate the potential of marine fungus Purpureocillium lilacinum isolated from an Indonesian marine sponge Stylissa sp. as an anti-obesity agent through pancreatic lipase inhibition assay. The fungus was identified as P. lilacinum through morphological and molecular characteristics. The fungal extract’s inhibition activity and kinetics were evaluated using spectrophotometry and Lineweaver-Burk plots. Ethyl acetate and butanol were used for extraction. Both extracts showed pancreatic lipase inhibition in a concentration-dependent manner. Both crude extracts were then fractionated once. All fractionated extracts showed inhibitory activity above 50%, with the highest activity found in fraction 5 of ethyl acetate at 93.41% inhibition. The best fractionated extract had an IC50value of 220.60 µg.mL-1. The most active fraction of P. lilacinum had a competitive-type inhibitor behavior as shown by the value of Vmax not significantly changing from 388.80 to 382.62 mM pNP.min-1, and the Michaelis-Menten constant (KM) increased from 2.02 to 5.47 mM in the presence of 500 µg.mL-1 fractionated extract. Metabolite identification with LC-MS/MS QTOF suggested that galangin, kaempferol, and quercetin were responsible for the observed lipase inhibition.

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Tarigan, Ronald, Nastiti Kusumorini, and Wasmen Manalu. "Effectivity of Immunoglobulin Y Anti Lipase as a Pancreatic Lipase Inhibitor for Prevention of Obesity*." Pakistan Journal of Nutrition 15, no. 7 (June 15, 2016): 625–32. http://dx.doi.org/10.3923/pjn.2016.625.632.

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Tarigan, Ronald, Nastiti Kusumorini, and Wasmen Manalu. "Effectivity of Immunoglobulin Y Anti Lipase as a Pancreatic Lipase Inhibitor for Prevention of Obesity*." Pakistan Journal of Nutrition 15, no. 8 (July 15, 2016): 752–59. http://dx.doi.org/10.3923/pjn.2016.752.759.

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Hirose, Mai, Taishi Ando, Rahman Shofiqur, Kouji Umeda, Yoshikatsu Kodama, Sa Nguyen, Tsuyoshi Goto, Masaya Shimada, and Satoshi Nagaoka. "Anti-obesity activity of hen egg anti-lipase immunoglobulin yolk, a novel pancreatic lipase inhibitor." Nutrition & Metabolism 10, no. 1 (2013): 70. http://dx.doi.org/10.1186/1743-7075-10-70.

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Hadváry, P., W. Sidler, W. Meister, W. Vetter, and H. Wolfer. "The lipase inhibitor tetrahydrolipstatin binds covalently to the putative active site serine of pancreatic lipase." Journal of Biological Chemistry 266, no. 4 (February 1991): 2021–27. http://dx.doi.org/10.1016/s0021-9258(18)52203-1.

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Martinez-Gonzalez, Alejandra Isabel, Ángel Gabriel Díaz-Sánchez, Laura Alejandra De la Rosa, Ismael Bustos- Jaimes, Alma A. Vazquez-Flores, and Emilio Alvarez-Parrilla. "Inhibición de lipasa pancreática por flavonoides: importancia del doble enlace C2=C3 y la estructura plana del anillo C//Inhibition of pancreatic lipase by flavonoids: relevance of the C2=C3 double bond and C-ring planarity." Biotecnia 22, no. 2 (March 21, 2020): 50–60. http://dx.doi.org/10.18633/biotecnia.v22i2.1245.

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Lipasa pancreática es una enzima clave en el metabolismo de lípidos. Los flavonoides son compuestos bioactivos de gran relevancia debido a sus interacciones con enzimas digestivas. Se evaluó la actividad de lipasa pancreática en presencia de flavonoides. Mediante espectroscopía UVVisible se determinó que el mejor inhibidor fue quercetina, seguido de rutina > luteolina > catequina > hesperetina, con valores de IC50 de 10.30, 13.50, 14.70, 28.50 y 30.50 μM, respectivamente. Todos los flavonoides mostraron una inhibición mixta, excepto catequina que mostró una inhibición acompetitiva. La capacidad inhibitoria de los flavonoides se relacionó con propiedades estructurales compartidas entre los distintos flavonoides, como la hidroxilación en las posiciones C5, C7 (anillo A), C2’ y C3’ (anillo B), y el doble enlace entre C2 y C3 (anillo C). Los resultados de inhibición coincidieron con el análisis de la fluorescencia extrínseca. Los estudios de docking molecular indicaron que la interacción entre lipasa pancreática y los flavonoides fue principalmente mediante interacciones hidrofóbicas (pi-stacking). Las interacciones de todos los flavonoides, excepto rutina, se dieron en el mismo sitio (subsitio 1) de la enzima. La insaturación entre C2 y C3 fue determinante para el acomodo de los flavonoides con la enzima, principalmente por interacciones de pi-stacking.ABSTRACTPancreatic lipase is a key enzyme in lipid metabolism. Flavonoids are bioactive compounds obtained from vegetables with big relevance, due to their intrinsic interaction with digestive enzymes. Pancreatic lipase activity was evaluated in the presence of flavonoids, through UV-Vis spectroscopy. All tested flavonoids showed a mixed-type inhibition, except catechin, which showed a uncompetitive inhibition. The best inhibitor was quercetin followed by rutin > luteolin > catechin > hesperetin, with IC50 values of 10.30, 13.50, 14.70, 28.50 and 30.50 μM, respectively. The flavonoids inhibitory capacity was related to structural properties shared between the different flavonoids, such as the hydroxylation at C5, C7 (ring A), C2’ and C3’ (ring B), and the double bond between C2 and C3 (ring C). The inhibition results are in agreement with the extrinsic fluorescence analysis. Molecular docking studies indicated that the interaction between pancreatic lipase and flavonoids was mainly through hydrophobic interactions (pi-stacking). The interactions of all flavonoids, except rutin, occurred at the same enzyme site (subsite 1). Instauration between C2 and C3 was decisive for the arrangement of flavonoids with the enzyme, mainly due to pi-stacking interactions.

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Appiah, Kingsley K., Yuval Blat, Barbara J. Robertson, Bradley C. Pearce, Donna L. Pedicord, Robert G. Gentles, Xuan-Chuan Yu, et al. "Identification of Small Molecules That Selectively Inhibit Diacylglycerol Lipase–α Activity." Journal of Biomolecular Screening 19, no. 4 (November 15, 2013): 595–605. http://dx.doi.org/10.1177/1087057113511111.

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Recent genetic evidence suggests that the diacylglycerol lipase (DAGL-α) isoform is the major biosynthetic enzyme for the most abundant endocannabinoid, 2-arachidonoyl-glycerol (2-AG), in the central nervous system. Revelation of its essential role in regulating retrograde synaptic plasticity and adult neurogenesis has made it an attractive therapeutic target. Therefore, it has become apparent that selective inhibition of DAGL-α enzyme activity with a small molecule could be a strategy for the development of novel therapies for the treatment of disease indications such as depression, anxiety, pain, and cognition. In this report, the authors present the identification of small-molecule inhibitor chemotypes of DAGL-α, which were selective (≥10-fold) against two other lipases, pancreatic lipase and monoacylglycerol lipase, via high-throughput screening of a diverse compound collection. Seven chemotypes of interest from a list of 185 structural clusters, which included 132 singletons, were initially selected for evaluation and characterization. Selection was based on potency, selectivity, and chemical tractability. One of the chemotypes, the glycine sulfonamide series, was prioritized as an initial lead for further medicinal chemistry optimization.

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Sarkar, Subha Jyoti, Divya Dioundi, and Mahiti Gupta. "ENDOPHYTIC PESTALOTIOPSIS SPECIES FROM ANDAMAN ISLANDS: A POTENTIAL PANCREATIC LIPASE INHIBITOR." Asian Journal of Pharmaceutical and Clinical Research 10, no. 10 (September 1, 2017): 82. http://dx.doi.org/10.22159/ajpcr.2017.v10i10.19795.

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Objective: Obesity is the major cause of deaths worldwide. Inhibition of enzymes involved in breakdown of fats can be a good way for obesity management. Pancreatic lipase (PL) causes 50-70% degradation of ingested fats. The aim of this work is to explore the endophytic fungi from untapped biodiversity of Andaman Islands for PL inhibitors.Methods: In the current report, culture broths of 39 endophytic fungi from different curative plants of coastal regions of India have been tested for their potential PL inhibitory activity. The bioactive compound was thus isolated, purified, and analyzed using gas chromatography.Results: It was found that inhibitory concentration of a compound (Rf=0.64) isolated from crude hexane extract of endophytic fungal isolate from Citrus limon was 15.46 μg/ml. Gas chromatogram of the extract showed the presence of caryophyllene which might be responsible for the particular activity. The bioactive fungus was microscopically identified as Pestalotiopsis species.Conclusion: As caryophyllene is component of many oils and is non-toxic, so it can be potential source of safe and effective anti-obesity drug.

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Aji, Oktira Roka, Riris Asyhar Hudaya, and Diah Asta Putri. "In Vitro Pancreatic Lipase Inhibitor Activity of Mangifera foetida Leaves Extract." Jurnal Biodjati 6, no. 1 (June 1, 2021): 82–92. http://dx.doi.org/10.15575/biodjati.v6i1.10646.

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Tsujita, Takahiro, Hiroe Takaichi, Takeshi Takaku, Shigeyuki Aoyama, and Jun Hiraki. "Antiobesity action of ϵ-polylysine, a potent inhibitor of pancreatic lipase." Journal of Lipid Research 47, no. 8 (May 24, 2006): 1852–58. http://dx.doi.org/10.1194/jlr.m600168-jlr200.

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PASQUALINI, Eric, Nathalie CAILLOL, Anne VALETTE, Roland LLOUBES, Alain VERINE, and Dominique LOMBARDO. "Phosphorylation of the rat pancreatic bile-salt-dependent lipase by casein kinase II is essential for secretion." Biochemical Journal 345, no. 1 (December 17, 1999): 121–28. http://dx.doi.org/10.1042/bj3450121.

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Bile-salt-dependent lipase (BSDL, EC 3.1.1.-) is an enzyme expressed by the pancreatic acinar cells and secreted as a component of the pancreatic juice of all examined species. During its secretion route BSDL is associated with intracellular membranes. This association allows the complete glycosylation of the enzyme or participates in the inhibition of the enzyme activity, which can deleterious for the acinar pancreatic cell. Thereafter, the human BSDL is phosphorylated by a serine/threonine protein kinase and released from intracellular membranes. In the present study, we show that the rat pancreatic BSDL, expressed by AR4-2J cells used as a model, is phosphorylated by a protein kinase that is insensitive to inhibitors of protein kinases A, C or G and that the phosphorylation process is favoured by okadaic acid (an inhibitor of protein phosphatases 1 and 2A). However, 5,6-dichloro-1-β-D-ribofuranosylbenzimidazole (DRB), which is a specific inhibitor of casein kinase II, abolishes the phosphorylation in vitro of BSDL within micro- somes of AR4-2J pancreatic cells. We showed further that the α-subunit of casein kinase II co-locates with BSDL within the lumenal compartment of the Golgi. Genistein, which perturbs the trans-Golgi network, also inhibits the phosphorylation of BSDL, suggesting that this post-translational modification of BSDL probably occurred within this cell compartment. The inhibition of the phosphorylation of BSDL by DRB also decreases the rate at which the enzyme is secreted. Under the same conditions, the rate of α-amylase secretion was not modified. These data strongly suggest that phosphorylation is a post-translational event, which appears to be essential for the secretion of BSDL.

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Naibaho, Frans Grovy, Ebrry Dwi Putra, Desimaria Panjaitan4, and Vinsen Willi Wardhana. "Analisis Molecular Docking Senyawa dari Jamur Endofit Bawang Dayak (Eleutherine bulbosa) Sebagai Inhibitor Lipase Pankreas." BIOSAINTROPIS (BIOSCIENCE-TROPIC) 7, no. 2 (January 29, 2022): 133–41. http://dx.doi.org/10.33474/e-jbst.v7i2.484.

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Nowadays some efforts are being made to reduce obesity by using drugs that aim to reduce appetite of the drug users. However, the use of drugs still has harmful side effects. Endophytic fungi originating from the Dayak onion plant are thought to have secondary metabolites that have potential as anti-obesity. The aims of this study were to determine the compounds produced by endophytic fungi of Dayak onion and to determine the potential components as inhibitors of pancreatic lipase enzymes. Samples of Dayak onions were collected from Palangka Raya using purposive sampling method. Isolation of endophytic fungi was conducted using surface sterilization method and the isolates were grown on PDA. Isolates were characterized and fermented on PDB for 14 days. The selected isolate was analyzed by using GCMS then molecular docking was performed using Autodock Vina and PyRx. The research results showed that there were 7 isolates of endophytic fungi isolated from leaves and roots tissues of Dayak onion. GCMS analysis showed that EBD1 contains 38 compounds. Molecular docking analysis showed that 1,3-Di-O-Acetylpentopyranose, a test ligand, has the closest binding affinity value (-6.6 kcal/mol) to orlistat (control) (-6.8 kcal/mol). Thus, it has the potential as an inhibitor of pancreatic lipase enzyme protein.

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Crass, R. A., P. S. Oatesa, and R. G. H. Morgan. "The effect of fasting on enzyme levels in the enlarged and involuting rat pancreas." British Journal of Nutrition 58, no. 3 (November 1987): 427–36. http://dx.doi.org/10.1079/bjn19870111.

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1. The effect on pancreatic digestive enzyme levels of fasting and changes from a diet containing trypsin inhibitor (raw soya-bean flour, RSF) to diets free of trypsin inhibitor (heated soya-bean flour, HSF, or commercial rat chow) was studied in rats for up to 7 d.2. In RSF-fed rats killed without fasting, enzyme levels were low, but after fasting for 24 h before killing there was a marked increase in all enzyme levels. Histological studies showed that pancreatic acinar cells from RSF-fed rats killed without fasting were devoid of zymogen granules, but following a 24 h fast there was a marked accumulation of zymogen granules which extend into the basal cytoplasm. Fasting either produced no change or a fall in enzyme levels in rats fasted after feeding HSF or chow continuously.3. If animals fed on RSF were changed to HSF and either fed or fasted for 24 h up to the time of killing there was an increase in amylase (EC3. 2. 1. 1), trypsin (EC3. 4. 21. 4), lipase (triacylglycerol lipase;EC3. 1. 1. 3) and protein 1 d after the change, followed by a fall over the next 6 d to levels similar to those seen in rats fed on HSF continuously.4. Animals changed from RSF to chow showed similar effects as far as trypsin, lipase and protein were concerned, but amylase rose, to reach the level seen in rats fed on chow continuously (about ten times that seen in soya-bean-fed rats), after 2 d.5. These results suggest that in the rats fed on RSF, pancreatic enzyme synthesis is rapid but secretion is equally rapid and intracellular enzyme levels are low. When these animals are fasted or changed to a diet free of trypsin inhibitor the rate of secretion falls but the high rate of synthesis continues for at least 24 h and enzymes accumulate in the pancreas. In studies of pancreatic enzyme levels in rats fed on trypsin inhibitor the extent of fasting before killing the animal is therefore an important variable. Such animals should probably not be fasted before study.

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Carrière, Frédéric, Christophe Renou, Stéphane Ransac, Véronique Lopez, Josiane De Caro, Francine Ferrato, Alain De Caro, et al. "Inhibition of gastrointestinal lipolysis by Orlistat during digestion of test meals in healthy volunteers." American Journal of Physiology-Gastrointestinal and Liver Physiology 281, no. 1 (July 1, 2001): G16—G28. http://dx.doi.org/10.1152/ajpgi.2001.281.1.g16.

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The inhibition of digestive lipases by the antiobesity drug Orlistat along with lipolysis levels and fecal fat excretion were measured in healthy humans. Orlistat was found to be a powerful gastric lipase inhibitor, achieving 46.6–91.4% enzyme inhibition and thus greatly reducing gastric lipolysis of solid and liquid meals (11–33% of respective controls). Gastric lipase inhibition by Orlistat was extremely fast (half-inhibition time < 1 min). Duodenal lipolysis was reduced significantly by Orlistat given with the solid meal (32.6–37.6% of controls) but was only slightly reduced by Orlistat given with the liquid meal (74.5–100% of controls). Human pancreatic lipase (HPL) inhibition was found to be high (51.2–82.6%), however, regardless of the meal. These paradoxical results were explained when in vitro lipolysis experiments were performed. The rates of HPL inhibition by Orlistat were found to be similar with both types of meals (half-inhibition time 5–6 min), but the preemulsified triglycerides of the liquid meal were rapidly hydrolyzed by HPL before the enzyme was significantly inhibited by Orlistat. With the solid meal, the rate of hydrolysis of the meal triglycerides by HPL was slower than the rate of HPL inhibition by Orlistat. As predicted from the previous results, the effects of Orlistat on fat excretion levels were found to be much greater with the solid (40.5–57.4% of ingested fat) than with the liquid (4.2–18.8%) test meal.

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Ackroff, K., and A. Sclafani. "Effects of the lipase inhibitor orlistat on intake and preference for dietary fat in rats." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 271, no. 1 (July 1, 1996): R48—R54. http://dx.doi.org/10.1152/ajpregu.1996.271.1.r48.

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Orlistat (Ols), a potent inhibitor of pancreatic lipase, was added to the fat source (1 or 4 mg Ols/g fat) of a macronutrient self-selection diet fed to adult female rats. The rats responded to the drug-induced reduction in fat absorption by decreasing their dietary fat intake and increasing their protein and carbohydrate intake in a dose-related manner. Total caloric intake also increased, but body weight gain was inhibited compared with the nondrug control group. When Ols was removed from the diet, nutrient selection, caloric intake, and body weight returned to control levels. In additional short-term experiments (30 min/day), rats developed a preference for a plain fat diet over an Ols-fat diet (4 mg/g fat) and also for a cue flavor paired with plain fat over a flavor paired with Ols-fat. Yet, when not given the choice, the rats consumed nearly as much Ols-fat as plain fat diet. These results indicate that, by reducing fat absorption, Ols reduced the attractiveness of dietary fat, although it did not make the fat diet aversive. In clinical use, lipase inhibitors may be effective in reducing dietary fat intake by reducing both the consumption and absorption of fat.

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Chiou, Antonia, Theodoros Markidis, Violetta Constantinou-Kokotou, Robert Verger, and George Kokotos. "Synthesis and Study of a Lipophilicα-Keto Amide Inhibitor of Pancreatic Lipase." Organic Letters 2, no. 3 (February 2000): 347–50. http://dx.doi.org/10.1021/ol991295s.

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Journal articles on the topic 'Pancreatic lipase inhibitor'

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