Protective effects of three structurally similar polyphenolic compounds against oxidative damage and their binding properties to human serum albumin

Zhang, Chuanying; Guan, Jiao; Zhang, Jiaxing; Yang, Jichen; Wang, Xiaoli; Peng, Xin

doi:10.1016/j.foodchem.2021.129118

Cited by 28 publications

(15 citation statements)

References 38 publications

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“…Figure S5 and Table S3 exhibit the 3D fluorescence spectra and the related characteristic parameters of free α-amylase/α-glucosidase and α-amylase–silibinin/α-glucosidase–silibinin systems, respectively. As shown in Figure S5, peak a and peak b corresponded to the Rayleigh scattering peak (λ em = λ ex ) and the second-order scattering peak (λ em = 2λ ex ), respectively. , Moreover, peak 1 (the strong fluorescence peak) primarily revealed the spectral behavior of Trp and Tyr residues . From Table S3, it could be found that an obvious reduction in the fluorescence intensity of peak 1 (for α-amylase, decreased by 28.65%; for α-glucosidase, decreased by 32.43%) was observed, and a red shift in the peak position was recorded (for the α-amylase–silibinin system, 3 nm; for the α-glucosidase–silibinin system, 4 nm) when silibinin was added into the enzyme solution.…”

Section: Resultsmentioning

confidence: 91%

Inhibition Mechanism of α-Amylase/α-Glucosidase by Silibinin, Its Synergism with Acarbose, and the Effect of Milk Proteins

Yang

Wang

et al. 2021

J. Agric. Food Chem.

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As a natural flavonolignan, silibinin is reported to possess multiple biological activities, while the inhibitory potential of silibinin on carbohydrate-hydrolyzing enzymes is still unclear. Therefore, in this study, the inhibitory effect and underlying mechanism of silibinin against α-amylase/α-glucosidase were investigated. The results indicated that silibinin showed a strong inhibitory efficiency against α-amylase/α-glucosidase in noncompetitive manners and exhibited synergistic inhibition against αglucosidase with acarbose. However, interestingly, the inhibitory effect of silibinin was significantly hindered in various milk proteinrich environments, but this phenomenon disappeared after simulated gastrointestinal digestion of milk proteins in vitro. Furthermore, silibinin could combine with the inactive site of α-amylase/α-glucosidase and change the microenvironment and secondary structure of the enzymes, thereby influencing the catalytic efficiency of enzymes. This research suggested that silibinin could be used as a novel carbohydrate-hydrolyzing enzyme inhibitor, and milk beverages rich in silibinin had the potential for further application in antidiabetic dietary or medicine.

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Section: Resultsmentioning

confidence: 91%

Inhibition Mechanism of α-Amylase/α-Glucosidase by Silibinin, Its Synergism with Acarbose, and the Effect of Milk Proteins

Yang

Wang

et al. 2021

J. Agric. Food Chem.

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“…sappan ) and is used in traditional Chinese medicine as an anti‐inflammatory agent. But the antioxidant activity of hematein is lower than that of brazilin 59 . The anticancer effects of the oxidized products brazilein and hematein warrant further investigation.…”

Section: Discussionmentioning

confidence: 91%

“…But the antioxidant activity of hematein is lower than that of brazilin. 59 The anticancer effects of the oxidized products brazilein and hematein warrant further investigation. Our docking study suggests that the chromatin binding protein BAF1 is a nuclear target for these two related natural products.…”

Section: Discussionmentioning

confidence: 99%

Molecular docking of brazilin and its analogs to barrier‐to‐autointegration factor 1 (BAF1)

Soeiro

Vergoten

Bailly

2022

Annals of the New York Academy of Sciences

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The tetracyclic phenolic compound brazilin, derived from the wood of Caesalpinia sappan, has been shown to bind to the chromatin protein BAF1 (barrier-to-autointegration factor 1), a protein essential to maintain integrity of the nuclear envelope in cells. BAF1 plays a role in cancer development. Using molecular docking, we have located the binding site for brazilin on the surface of the BAF1 monomer and compared its binding to that of four analogs. The oxidized product brazilein ( E = −57.7 kcal/mol) exhibits a higher affinity for BAF1 compared to the reduced form brazilin ( E = −38.2 kcal/mol). Incorporation of a 4-hydroxyl substituent on the indenochromene unit affords hematoxylin and hematein. In silico analysis predicts that the oxidized form hematein ( E = −66.2 kcal/mol) displays a higher affinity for BAF1 than the reduced form hematoxylin ( E = −42.2 kcal/mol). In contrast, the atypical bis-lactone product brazilide A cannot form good complexes with BAF1. The analysis points to the formation of more stable BAF1 complexes with the oxidized molecules compared to the reduced ones, but the position of the binding site on the protein cavity is different for brazilin/hematoxylin compared to brazilein/hematein. Our study may be useful to guide the design of BAF1 ligands.

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“…Consequently, the interaction with specific binding sites of ANT can underlie the influence of different agents on MPTP. It can be assumed that the effect of agrimoniin on adenylate translocase is mediated by the binding of its hydroxyl groups to individual amino acid residues of the transporter, as has been shown for other proteins and tannins [4][5][6][7][8]. This assumption is supported by our data showing that, despite the high antioxidant activity inherent in this group of compounds, agrimoniin induces swelling in the absence of other activating factors, such as an excess of calcium, reactive oxygen species, and various oxidants, which fix ANT in the c-state and stimulate MPTP opening.…”

Section: Discussionmentioning

confidence: 99%

“…These effects are believed to be mediated primarily by direct binding to specific proteins and enzymes. The binding of tannins to phosphatase [4], pyruvate kinase [5], gluten proteins [6], albumin [7], and deacetylase [8] was revealed. It was shown that the binding of tannins to kinases and phosphatases led to changes in the level of kinase phosphorylation and, accordingly, the activity of signaling pathways involved in the regulation of proliferation and apoptosis [9].…”

Section: Introductionmentioning

confidence: 99%

New Properties and Mitochondrial Targets of Polyphenol Agrimoniin as a Natural Anticancer and Preventive Agent

2021

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Agrimoniin is a polyphenol from the group of tannins with antioxidant and anticancer activities. It is assumed that the anticancer action of agrimoniin is associated with the activation of mitochondria-dependent apoptosis, but its mitochondrial targets have not been estimated. We examined the direct influence of agrimoniin on different mitochondrial functions, including the induction of the mitochondrial permeability transition pore (MPTP) as the primary mechanism of mitochondria-dependent apoptosis. Agrimoniin was isolated from Agrimonia pilosa Ledeb by multistep purification. The content of agrimoniin in the resulting substance reached 80%, as determined by NMR spectroscopy. The cytotoxic effect of purified agrimoniin was confirmed on the cultures of K562 and HeLa cancer cells by the MTT assay. When tested on isolated rat liver mitochondria, agrimoniin at a low concentration (10 µM) induced the low-amplitude swelling, which was inhibited by the MPTP inhibitors ADP and cyclosporine A, activated the opening of MPTP by calcium ions and stimulated the respiration supported by succinate oxidation. Also, agrimoniin reduced the electron acceptor DCPIP in a concentration-dependent manner and chelated iron ions. Owing to all these properties, agrimoniin can stimulate apoptosis or activate mitochondrial functions, which can be helpful in the prevention and elimination of stagnant pathological states.

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Protective effects of three structurally similar polyphenolic compounds against oxidative damage and their binding properties to human serum albumin

Cited by 28 publications

References 38 publications

Inhibition Mechanism of α-Amylase/α-Glucosidase by Silibinin, Its Synergism with Acarbose, and the Effect of Milk Proteins

Inhibition Mechanism of α-Amylase/α-Glucosidase by Silibinin, Its Synergism with Acarbose, and the Effect of Milk Proteins

Molecular docking of brazilin and its analogs to barrier‐to‐autointegration factor 1 (BAF1)

New Properties and Mitochondrial Targets of Polyphenol Agrimoniin as a Natural Anticancer and Preventive Agent

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