Characterization of the synergistic inhibitory effect of cyanidin-3-O-glucoside and catechin on pancreatic lipase

Wang, Yuying; Chen, Lihang; Liu, Huimin; Xie, Jiahan; Yin, Wandi; Xu, Zhenghang; Ma, Huan; Wu, Wenzhuo; Zheng, Mingzhu; Liu, Meihong; Liu, Jingsheng

doi:10.1016/j.foodchem.2022.134672

Cited by 20 publications

(10 citation statements)

References 33 publications

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“…The family of compounds showing the strongest effect were the di-caffeoylquinic acids with 4.8, 6.2, 7.2, 9.4, and 11.4 times higher inhibitory activities on α-amylase than acarbose for cynarin, 1,5-dicaffeoylquinic acid, 3,4-dicaffeoylquinic acid, 3,5-dicaffeoylquinic acid, and 4,5-dicaffeoylquinic acid, respectively (based on IC 50 values) [ 51 ]. Similarly, significant lipase inhibitory activities have been shown for apigenin, oleanolic acid, anthocyanins, monocaffeoylquinic acids (including chlorogenic acid), dicaffeoylquinic acids (including cynarin), luteolin-7-O-glucoside, luteolin, and Eriodictyol [ 63 , 64 , 65 , 66 , 67 , 68 ]. The highest lipase inhibitions were obtained using luteolin-7-O-glucoside and eriodictyol, two flavonoids, with more than two times higher inhibitory activities than orlistat for both (based on IC 50 values) [ 68 ].…”

Section: Discussionmentioning

confidence: 99%

Inhibitory Potential of α-Amylase, α-Glucosidase, and Pancreatic Lipase by a Formulation of Five Plant Extracts: TOTUM-63

Haguet

Joubioux

Chavanelle

et al. 2023

IJMS

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Controlling post-prandial hyperglycemia and hyperlipidemia, particularly by regulating the activity of digestive enzymes, allows managing type 2 diabetes and obesity. The aim of this study was to assess the effects of TOTUM-63, a formulation of five plant extracts (Olea europaea L., Cynara scolymus L., Chrysanthellum indicum subsp. afroamericanum B.L.Turner, Vaccinium myrtillus L., and Piper nigrum L.), on enzymes involved in carbohydrate and lipid absorption. First, in vitro inhibition assays were performed by targeting three enzymes: α-glucosidase, α-amylase, and lipase. Then, kinetic studies and binding affinity determinations by fluorescence spectrum changes and microscale thermophoresis were performed. The in vitro assays showed that TOTUM-63 inhibited all three digestive enzymes, particularly α-glucosidase (IC50 of 13.1 µg/mL). Mechanistic studies on α-glucosidase inhibition by TOTUM-63 and molecular interaction experiments indicated a mixed (full) inhibition mechanism, and higher affinity for α-glucosidase than acarbose, the reference α-glucosidase inhibitor. Lastly, in vivo data using leptin receptor-deficient (db/db) mice, a model of obesity and type 2 diabetes, indicated that TOTUM-63 might prevent the increase in fasting glycemia and glycated hemoglobin (HbA1c) levels over time, compared with the untreated group. These results show that TOTUM-63 is a promising new approach for type 2 diabetes management via α-glucosidase inhibition.

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Section: Discussionmentioning

confidence: 99%

Inhibitory Potential of α-Amylase, α-Glucosidase, and Pancreatic Lipase by a Formulation of Five Plant Extracts: TOTUM-63

Haguet

Joubioux

Chavanelle

et al. 2023

IJMS

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“…The effect of the individual catechins on PPL determined by using olive oil as a substrate may be required to further confirm these results. Moreover, the most recent study has revealed that catechins as non-competitive inhibitors could enhance the inhibitory effect of cyanidin-3-glucoside (C3G), a competitive inhibitor on PPL via the catechin-C3G mixture [28] . Further investigations of the synergistic PPL inhibitory activity of catechin-EGC and catechin-EC mixtures have garnered significant interest.…”

Section: Discussionmentioning

confidence: 99%

“…The protein was converted from ‘pdb’ to a ‘pdbqt’ format using Python script (Prepare_receptor4.py) the AutoDock Tool (ADT) and the metal charges were then automatically calculated (e.g., zinc ion = +2.0). Resolution of the three-dimensional grid box ( x , y , and z ) was set at 26 × 34 × 36 for the active pocket [27] and 22 × 30 × 28 for the catechin binding pocket [28] with a grid spacing of 0.375 Å. The center of the grid was set to 56.658, 47.892, and 122.042 Å for the × , y , and z dimensions of the active site and 63.305, 27.761, and 149.683 Å for the × , y , and z dimensions of the catechin binding site, respectively.…”

Section: Methodsmentioning

confidence: 99%

Ultrasonic-assisted enzymatic improvement of polyphenol content, antioxidant potential, and in vitro inhibitory effect on digestive enzymes of Miang extracts

Leangnim

Unban

Thangsunan

et al. 2023

Ultrasonics Sonochemistry

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“…A molecular docking study stated that cyanidin-3-o-glucoside had a binding value of -7.038 and -12.872 against pancreatic lipase and glucosidase enzymes in the hydrolases family, respectively. [44,45]…”

Section: Antibacterial Potency Of Endemic Plant Extractsmentioning

confidence: 99%

Evaluation of Biological Potency of two Endemic Species Integrated with in vitro and in silico Approches: LC–MS/MS Analysis of the Plants

Kısa,

Baş Topcu,

Tunçkol

et al. 2024

Chemistry & Biodiversity

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In the present study, the main phytochemical components of endemic plant extracts and inhibitory potency were screened related to different biological activities. Seven compounds were quantified, and cyanidin‐3‐o‐glucoside was the dominant secondary metabolite in plant extracts. The extract from P. asiae‐minoris (PAM) exhibited the best enzyme inhibitory activity against BChE (1.73±0.23 µg mLˉˡ), tyrosinase (2.47±0.28 µg mLˉˡ), α‐glucosidase (5.28±0.66 µg mLˉˡ), AChE (8.66±0.86 µg mLˉˡ), and ACE (19.27±1.02 µg mLˉˡ). In vitro antioxidant assay, PAM extract possessed the highest activity in respect of DPPH radical scavenging (24.29±0.23 µg/mL), ABTS•+ scavenging (13.50±0.27 µg/mL) and FRAP reducing power (1.56±0.01 μmol TE/g extract). MIC values ranged from 1 ‐ 8 mg/mL for antibacterial ability, and the PAM extract showed a stronger effect for B. subtilis, E. faecalis, and E. coli at 1 mg/mL. The antiproliferative ability of AB extract demonstrated a suppressive effect (IC50: 70.26 µg/mL) for pancreatic cancer cell lines. According to the affinity scores, the cyanidin‐3‐o‐glucoside demonstrated the lowest docking scores against ACE, AChE, BChE, and collagenase. It was found that the PAM exhibited better inhibitory capabilities than A. bartinense. The P. asiae‐minoris, reported to be in the Critically Endangered (CR) category, should be conserved by culturing, considering its biological abilities.

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Characterization of the synergistic inhibitory effect of cyanidin-3-O-glucoside and catechin on pancreatic lipase

Cited by 20 publications

References 33 publications

Inhibitory Potential of α-Amylase, α-Glucosidase, and Pancreatic Lipase by a Formulation of Five Plant Extracts: TOTUM-63

Inhibitory Potential of α-Amylase, α-Glucosidase, and Pancreatic Lipase by a Formulation of Five Plant Extracts: TOTUM-63

Ultrasonic-assisted enzymatic improvement of polyphenol content, antioxidant potential, and in vitro inhibitory effect on digestive enzymes of Miang extracts

Evaluation of Biological Potency of two Endemic Species Integrated with in vitro and in silico Approches: LC–MS/MS Analysis of the Plants

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