Inhibition study of red rice polyphenols on pancreatic α-amylase activity by kinetic analysis and molecular docking

Liu, Mei; Hu, Bo; Zhang, Hui; Zhang, Yu; Wang, Li; Qian, Haifeng; Qi, Xiguang

doi:10.1016/j.jcs.2017.04.011

Cited by 51 publications

(21 citation statements)

References 28 publications

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“…Although orally administered OeB has some physical activity, this can be affected by many factors, including the extensive enzymatic and chemical modifications that occur during digestion and absorption (Scheepens, Tan, & Paxton, 2010). Previous studies have noted that most polyphenolic compounds from medicinal herbs can strongly interact with globular proteins, including digestive enzymes, which may reduce food digestibility (Han et al, 2008;Liu et al, 2017;Miao, Jiang, Jiang, Zhang, & Li, 2015;Rohn, And, & Kroll, 2002). As a macromolecular polyphenolic compound, OeB will inevitably interact with digestive tract enzymes in the body after oral administration, which may also influence the activity of digestive enzymes.…”

Section: Introductionmentioning

confidence: 99%

Investigation on the Interaction Behavior Between Oenothein B and Pepsin by Isothermal Titration Calorimetry and Spectral Studies

Liu

Wang

Shi

et al. 2019

Journal of Food Science

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Oenothein B (OeB) is a dimeric macrocyclic ellagitannin isolated from Herbs and fruits that have a variety of biological activities. In order to better understand the effect of OeB on the activity of the digestive enzyme pepsin, interactions between OeB and pepsin were investigated in vitro under simulated physiological conditions based on enzyme inhibition studies, fluorescence, isothermal titration calorimetry, CD, and molecular docking. It was found OeB is an effective inhibitor of pepsin, likely acting in a reversible manner through both competitive and noncompetitive inhibition. Fluorescence quenching of pepsin by OeB was a static quenching. CD spectra showed the addition of OeB causes the main chain of pepsin to loosen and expand and the partial β‐sheet structure to be converted to a disordered structure. Isothermal titration calorimetry and docking studies revealed the main binding mechanism of OeB and pepsin was through noncovalent interactions, hydrophobic interactions with OeB and the internal hydrophobic group of pepsin, and then hydrogen bonding between OeB and the Val243 and Asp77 residues of pepsin. Noncovalent bonds between OeB and pepsin change the polarity and structure of enzymes, decreasing enzymatic activity. Compared with small molecular polyphenols, OeB has a weaker hydrophobic interaction with pepsin and less effect on the secondary structure of pepsin. These findings are the first direct elucidation of the interactions between the oligomer ellagitannin OeB and pepsin, further contributing to understanding binding between oligomer ellagitannins and digestive enzymes. Practical Application The results of this study indicate that the interaction between OeB and pepsin has a certain inhibitory effect on pepsin. In order to reduce the impact of OeB on human digestion and its own activities, nano‐encapsulation technology can be used in the future to protect oligomeric ellagitannin such as OeB.

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Section: Introductionmentioning

confidence: 99%

Investigation on the Interaction Behavior Between Oenothein B and Pepsin by Isothermal Titration Calorimetry and Spectral Studies

Liu

Wang

Shi

et al. 2019

Journal of Food Science

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“…Recently, in silico analyses (also known as molecular modeling or docking) have been used as a relevant and unique tool to explain or predict dynamics and mechanisms of enzymatic inhibition, providing information about specific interactions and conformation of protein–inhibitor complexes at atomic level (Escobedo‐González et al., ; Liu et al., ; Zhou et al., ; Martínez Gonzalez, Alvarez‐Parrilla, et al., ; Chai et al., ). In this study, we performed molecular dockings for the three digestive enzymes: pancreatic α‐amylase, lipase, and trypsin and their binding with model PACs from C. illinoinensis .…”

Section: Introductionmentioning

confidence: 99%

“…Figure shows the molecular docking simulations (UCSF Chimera 1.12v software) of the interaction between the four model PACs and pancreatic α‐amylase, simulations with other enzymes showed similar behavior, although the interaction with α‐amylase presented the clearest tendency. Pancreatic α‐amylase is one of the α‐glucosidases recently recognized as therapeutic target for the prevention and control of diabetes mellitus type 2 (Liu et al., ); it hydrolyzes α‐1‐4 glycosidic linkages in starch, and its active site contains a catalytic triad formed by Asp 197 , Glu 233 , and Asp 300 . Figure shows that trimeric and tetrameric PACs bound with amino acid residues from this triad: kernel PACs (trimer and tetramer) bound with Asp 197 and Asp 300 (Figure A and B), while the shell tetramer interacted with Asp 300 and Glu 233 (Figure D).…”

Section: Introductionmentioning

confidence: 99%

Proanthocyanidins with a Low Degree of Polymerization are Good Inhibitors of Digestive Enzymes Because of their Ability to form Specific Interactions: A Hypothesis

Vazquez-Flores¹,

Martinez-Gonzalez²,

́Álvarez-Parrilla³

et al. 2018

Journal of Food Science

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Inhibition of target digestive enzymes is an accepted strategy to prevent diseases such as obesity and diabetes. Proanthocyanidins (PACs) are known for their ability to bind, inhibit, and precipitate enzymes, which makes them potential bioDrugs with an impact on the digestive process. PAC degree of polymerization (DP) is one of the structural features responsible for their differential inhibitory potency but the explanation for this phenomenon is still unclear. Pecan nut (Carya illinoinensis L.) kernels and nutshells are rich in oligomeric and polymeric PACs. We have used thiolysis and HPLC analyses to propose four theoretical model structures of PACs representative of four semipurified fractions obtained from pecan kernel and shell, which showed different inhibitory activity against intestinal lipases, amylases, and proteases. The noncovalent interactions between PACs and digestive enzymes were predicted by in silico methods through computational software. These observations are discussed in view of current literature on the biological effects of PACs with different DPs and allowed us to propose the hypothesis that "small oligomeric PACs could be digestive enzyme inhibitors due to their capacity to enter and bind the enzymes' specific cavities better than polymers and oligomers of medium and high molecular weight."

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“…The first one is due to the inhibitory action on mammal digestive enzymes such as α-amylase and α-glucosidase of various classes of camu-camu fruit extracts rich in polyphenolic compounds [22,25,72]. These bioactive compounds shown different inhibition mechanisms against these enzymes by binding to free enzyme and/or enzyme-substrate complexes, causing competitive inhibition, noncompetitive inhibition, and/or mixed-type inhibition [73][74][75][76]. The second one is a result of the inhibitory action on intestinal sugar transporters (i.e., SGLT1 and GLUT2), which was demonstrated in several studies [77][78][79][80][81][82].…”

Section: Hypoglycemiant and Antidiabetic Activitiesmentioning

confidence: 99%

Bioactive Compounds of Camu-Camu (Myrciaria dubia (Kunth) McVaugh)

Castro

Maddox

Cobos³

et al. 2019

Reference Series in Phytochemistry

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Camu-camu is a shrub, native to the Amazon that thrives in areas where flooding is frequent. Genetically, the plant is characterized by a diploid genome and moderate genetic diversity. Several parts of the plant are used in traditional folk medicine to treat a variety of acute and chronic diseases. For over 50 years, the exceptionally high vitamin C content of camu-camu has attracted worldwide attention that continues today because of the recent discovery of several healthpromoting phytochemicals with corroborated biological activities (e.g., antioxidant, anti-obesity, antidiabetic). All of these beneficial attributes are well supported by in vitro and in vivo studies as well as human clinical trials. The metabolic precursors of these phytochemicals are synthesized in key metabolic pathways (i.e., the shikimate pathway, the mevalonate pathway). Of these metabolic pathways, we show details for the biosynthesis of betulinic acid, transresveratrol, and syringic acid. In conclusion, camu-camu is an exceptional plant for its ability to produce and accumulate significant amounts of a variety of health-promoting phytochemicals. Although several metabolic pathways responsible for the biosynthesis of these phytochemicals have been reconstructed based on fruit and seedling transcriptomes, detailed knowledge of the vast majority of metabolic pathways and their molecular regulatory mechanisms is lacking. Consequently, we must increase our knowledge of the metabolic processes using multi-omic approaches so that we can acquire the skills necessary to develop genetically improved varieties of camu-camu and implement biotechnological applications for the production of these bioactive phytochemicals.

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Inhibition study of red rice polyphenols on pancreatic α-amylase activity by kinetic analysis and molecular docking

Cited by 51 publications

References 28 publications

Investigation on the Interaction Behavior Between Oenothein B and Pepsin by Isothermal Titration Calorimetry and Spectral Studies

Investigation on the Interaction Behavior Between Oenothein B and Pepsin by Isothermal Titration Calorimetry and Spectral Studies

Proanthocyanidins with a Low Degree of Polymerization are Good Inhibitors of Digestive Enzymes Because of their Ability to form Specific Interactions: A Hypothesis

Bioactive Compounds of Camu-Camu (Myrciaria dubia (Kunth) McVaugh)

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