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procyanidin
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES · 2019 · IF 4.784

Investigation the interaction between procyanidin dimer and α-glucosidase: Spectroscopic analyses and molecular docking simulation

Taotao Dai,Jun Chen,David Julian McClements,Ti Li,Chengmei Liu

Procyanidins are reported to inhibit α-glucosidase, which may be a useful attribute for developing functional foods that control post-prandial blood sugar levels. At present, the nature of the molecular interaction between procyanidins and α-glucosidase is poorly understood. In this study, spectroscopic analyses and computer simulations were used to investigate the interactions between α-glucosidase and B-type procyanidin dimer (BPD). Our results suggest that BPD binds to α-glucosidase through a combination of hydrophobic and hydrophilic interactions. This hypothesis was based on measurements of the intrinsic fluorescence quenching, conformational changes, and surface hydrophobicity of the α-glucosidase after binding. Thermodynamic analysis suggested that α-glucosidase had one binding site for BPD and that the interaction was spontaneous. Homologous modeling of α-glucosidase was used to provide information about the precise nature of the molecular interactions. Molecular docking analysis suggested that BPD formed hydrogen bonds and hydrophobic interactions with α-glucosidase when it bound to its active site. This research offers new insights into the mechanism of interaction between procyanidins and α-glucosidase, which may be useful for the development of functional foods to tackle type 2 diabetes.

CAS / MDL: 29106-49-8
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FOOD AND CHEMICAL TOXICOLOGY · 2018 · IF 3.977

Procyanidin B2 protects against d-galactose-induced mimetic aging in mice: Metabolites and microbiome analysis

Ying Xiao,Jialin Dong,Zhiting Yin,Qiguo Wu,Yiming Zhou,Xiaoli Zhou

To elucidate the possible mechanisms for the preventive effect of procyanidin B2 on aging, a combined analysis of metabolic profile and gut microbiome was carried out in the present study. The mimetic aged mice induced by d -galactose injection (500 mg/kg, sc daily), and the preventive group was fed with the diet plus 0.2% procyanidin B2. After 7 weeks of treatment, the spatial memory was assayed using the Morris water maze test. Procyanidin B2 significantly ameliorated the impaired memory and antioxidant abilities induced by d -galactose. Furthermore, metabolomics analysis of plasma based on LC/Q-TOF-MS demonstrated that phosphatidyl cholines , oleic acid , linoleic acid , carnitine , pantothenic acid , and taurocholic acid were significantly increased in the mice treated with procyanidin B2, and pyruvic acid , hydroxybutyric acid , hippuric acid , and cholic acid were decreased significantly. Together, gut microbiome analysis using Illumina sequencing showed that there were significant differences in the Firmicutes / Bacteroidetes ratio and abundance of Roseburia , Lachnospiraceae , and Bifidobacterium between the aging and supplemental procyanidin B2 groups. In summary, procyanidin B2 possessed potential prevention of the cognitive and oxidative impairment via the metabolic pathway regulation related to citrate cycle, fatty acid, and bile acid in the aged mice, accompanied by remodeling the gut flora.

CAS / MDL: 3646-73-9
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INDUSTRIAL & ENGINEERING CHEMISTRY RESEARCH · 2014 · IF 2.235

Reduction of Hexavalent Chromium Using Recyclable Pt/Pd Nanoparticles Immobilized on Procyanidin-Grafted Eggshell Membrane

Miao Liang,Rongxin Su,Wei Qi,Yi Zhang,Renliang Huang,Yanjun Yu,Libing Wang,Zhimin He

Efficient immobilization of catalytic active metal nanoparticles into porous supporting materials is of important scientific interest in practice. We report on the fabrication of novel bionanocomposites, comprising a three-dimensional porous eggshell membrane (ESM) bioscaffold decorated with catalytic active metal (Pt, Pd) nanoparticles, to reduce highly toxic Cr(VI). Procyanidin (Pro), a natural plant polyphenol with abundant phenolic hydroxyls, was first covalently grafted on the ESM fiber surface to provide stable binding sites for chelating metal precursors. Highly dispersed Pt and Pd nanoparticles with small size were facilely generated and stably immobilized onto the surface of ESM followed by NaBH4 reduction. These metal nanoparticle-incorporating ESM composites were active heterogeneous catalysts for the reduction of toxic Cr(VI) to Cr(III) by employing formic acid as the reducing agent. Notably, it is easy to recover and recycle the catalysts, revealing the good stabilization of procyanidin-grafted ESM for nanoparticles.

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Materials Today Bio · 2024 · IF 8.7

Procyanidin capsules provide a new option for long-term ROS scavenging in chronic inflammatory diseases

Linxiao Sun,Shaoyin Wei,Chenglong Wang,Yipiao Zhang,Xingjie Zan,Lianxin Li,Chunwu Zhang

Chronic inflammatory diseases such as diabetic wounds and osteoarthritis are significant threats to human health. Failure to scavenge longstanding excessive reactive oxygen species (ROS) is an important cause of chronic inflammatory diseases, yet existing treatments that provide long-lasting therapeutic effects are limited. Here, procyanidin capsules were synthesized in a simple one-step way using calcium carbonate as a template. The biosafety of procyanidin capsules in vitro and in vivo was monitored by cytotoxicity and pathological sections. The therapeutic effect of procyanidin capsules in diabetic wounds and osteoarthritis was accessed by pathological evaluation combined with the quantification of inflammatory markers. The data showed that procyanidin capsules could long-term scavenge excessive ROS and effectively promote articular cartilage repair in osteoarthritis, accelerating diabetic wound healing. Lastly, transcriptome analysis suggested that procyanidin capsules commonly regulated adenosine 5′-monophosphate (AMP)-activated protein kinase (AMPK) signaling in diabetic wounds and osteoarthritis. This study provides a straightforward protocol for creating procyanidin capsules, while presenting a promising new therapeutic option for long-term scavenging ROS in chronic inflammatory diseases.

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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES · 2018 · IF 3.909

Investigation the interaction between procyanidin dimer and α-amylase: Spectroscopic analyses and molecular docking simulation

Taotao Dai,Jun Chen,Qian Li,Panying Li,Peng Hu,Chengmei Liu,Ti Li

Procyanidins were reported to have an inhibitory effect on α-amylase, but the interaction mechanism between procyanidins and α-amylase was rarely reported. Spectroscopic and molecular docking techniques were utilized to explore the interaction between porcine pancreatic α-amylase (PPA) and B-type procyanidin dimer (PB2). PB2 decreased the intrinsic fluorescence and surface hydrophobicity of PPA, indicating that an interaction occurred and complex formed. The binding process of complex was spontaneous and the main interaction was hydrophobic force. Circular dichroism showed conformational changes of PPA with an increasing of α-helix and β-sheet structure. Molecular docking speculated that PB2 could form hydrophobic force with PPA by bind to the active sit (Asp 167, Asn 100, Arg 158, His 201). This research can offer new insights into the mechanism of PB2 in inhibiting PPA catalysis and provide useful information on dietary recommendation of PB2 for the treatment of type 2 diabetes.

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PHYTOMEDICINE · 2025 · IF 8.3

Procyanidin C1 ameliorates aging-related skin fibrosis through targeting EGFR to inhibit TGFβ/SMAD pathway

Jun-Han Wang,Min Li,Peng-Fei Xie,Jia-Yao Si,Zhen-Jie Feng,Chuan-Feng Tang,Jian-Mei Li

Background Aging-related skin fibrosis (SF) is a complex condition with limited treatment options. Procyanidin C1 (PCC1), a natural polyphenolic compound with demonstrated senolytic activity, has emerged as a potential therapeutic agent for fibrotic disorders through its selective elimination of senescent cells. However, its therapeutic efficacy and mechanisms in aging-related SF remain unclear. Purpose This study aimed to investigate the mechanisms of PCC1 in aging-related SF. Results In D-galactose-induced L929 cells, PCC1 treatment significantly attenuated the expression of both senescence-associated markers (IL-1β, P16, P21 and LMNB1) and fibrosis-related markers (α-SMA, LOXL2 and COL1). Network pharmacology and experimental validation (molecular docking, DARTS, CETSA, MST) identified EGFR as a primary target, with PCC1 directly binding to and inhibiting EGFR phosphorylation. Furthermore, PCC1 treatment effectively down-regulated TGFβ1 expression and suppressed SMAD2/3 phosphorylation in D-galactose-induced L929 cells. Notably, PCC1 blocked NSC228155-induced EGFR phosphorylation and inhibited ERK/MAPK, AKT/mTOR and TGFβ/SMAD pathway activation. In bleomycin-induced SF mice, PCC1 significantly attenuated epidermal hyperplasia, improved collagen structure, restored the collagen I/III ratio, and reduced EGFR phosphorylation along with TGFβ1 expression and SMAD2/3 phosphorylation. Conclusion This study elucidates that PCC1 exerts its anti-fibrotic effects through dual mechanisms: resistance to cellular senescence and modulation of fibroblast heterogeneity. By directly binding to EGFR and inhibiting its phosphorylation, PCC1 subsequently suppresses multiple downstream signaling cascades, ultimately ameliorating TGFβ/SMAD-mediated SF. These findings establish PCC1 as a promising therapeutic candidate for aging-related skin fibrosis, offering a novel approach through targeted EGFR inhibition and comprehensive pathway modulation .

CAS / MDL: 3646-73-9 9036-06-0
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MICROCHEMICAL JOURNAL · 2021 · IF 4.821

Green synthesis, characterization of procyanidin-mediated gold nanoparticles and its application in fluorescence detection of prazosin

Dan Liu,Ruizhuo Lin,Huifang Wu,Jiahui Ji,Donghan Wang,Zhiyuan Xue,Shilan Feng,Xinyue Chen

Grape seed procyanidin extract was used to green synthesize AuNPs (OPC-AuNPs), in which procyanidin (OPC) accounted for 95% of total content. To improve the dispersion and uniformity of particle size, various conditions were optimized. The final OPC-AuNPs showed excellent stability and were characterized by a series of techniques. Owing to the good quenching properties of OPC-AuNPs, the fluorescence system of OPC-AuNPs and Rhodamine B (RB) mixture was established for prazosin testing. OPC-AuNPs could effectively quench fluorescence based on fluorescence resonance energy transfer (FRET). When prazosin and the testing system of OPC-AuNPs and RB mixture coexisted in the solution, prazosin would replace RB and competitively bond on the surface of OPC-AuNPs, thus RB was dissociated from OPC-AuNPs, resulting in the rapid recovery of fluorescence. This article provided a green, simple one-pot synthesis method for OPC-AuNPs and established a fast, sensitive, visible fluorescence system for prazosin detection which was successfully applied in real sample detection.

CAS / MDL: 7789-39-1
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FOOD CHEMISTRY · 2020 · IF 6.306

Protein-polyphenol functional ingredients: The foaming properties of lactoferrin are enhanced by forming complexes with procyanidin

Changhong Li,Taotao Dai,Jun Chen,Xin Li,Ti Li,Chengmei Liu,David Julian McClements

The solution turbidity and intrinsic fluorescence quenching increased after procyanidin was mixed with lactoferrin. The addition of procyanidin also caused a reduction in the surface hydrophobicity of the lactoferrin, suggesting procyanidin bound to non-polar patches on lactoferrin’s surfaces. Moreover, the binding interaction caused an appreciable alteration in the structure of both the polyphenol and protein. Thermodynamic analysis indicated the interaction was spontaneous and mainly driven by entropy changes, suggesting that hydrophobic interactions dominated. A computational docking simulation provided insights into the location of the most-likely binding sites on the protein, as well as the nature of the interaction forces involved. In particular, both hydrophobic and hydrogen bonding were found to be important. The binding of the procyanidin to the lactoferrin enhanced its foaming properties. These results may lead to the development of a new class of natural functional ingredients that can be used in food products to improve their quality attributes.

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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES · 2023 · IF 8.2

Investigation of peanut allergen-procyanidin non-covalent interactions: Impact on protein structure and in vitro allergenicity

Qin Geng,Ying Zhang,David Julian McClements,Wenlong Zhou,Taotao Dai,Zhihua Wu,Hongbing Chen

Interactions between plant polyphenols and food allergens may be a new way to alleviate food allergies. The non-covalent interactions between the major allergen from peanut (Ara h 2) with procyanidin dimer (PA2) were therefore characterized using spectroscopic, thermodynamic, and molecular simulation analyses. The main interaction between the Ara h 2 and PA2 was hydrogen bonding. PA2 statically quenched the intrinsic fluorescence intensity and altered the conformation of the Ara h 2, leading to a more disordered polypeptide structure with a lower surface hydrophobicity . In addition, the in vitro allergenicity of the Ara h 2-PA2 complex was investigated using enzyme-linked immunosorbent assay (ELISA) kits. The immunoglobulin E (IgE) binding capacity of Ara h 2, as well as the release of allergenic cytokines, decreased after interacting with PA2. When the ratio of Ara h 2-to-PA2 was 1:50, the IgE binding capacity was reduced by around 43 %. This study provides valuable insights into the non-covalent interactions between Ara h 2 and PA2, as well as the potential mechanism of action of the anti-allergic reaction caused by binding of the polyphenols to the allergens.

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Frontiers in Immunology · 2018 · IF 5.511

The Antioxidant Procyanidin Reduces Reactive Oxygen Species Signaling in Macrophages and Ameliorates Experimental Colitis in Mice

Chen Lu,You Qian,Hu Liang,Gao Jian,Meng Qianqian,Liu Wentao,Wu Xuefeng,Xu Qiang

Management of inflammatory bowel disease (IBD) is a real clinical challenge. Despite intense investigation, the mechanisms of IBD remain substantially unidentified. Some inflammatory conditions, such as matrix metalloproteinases (MMPs) and the nuclear factor-κB (NF-κB) and NOD-like receptor protein 3 (NLRP3) inflammasome signaling pathways, are reported to contribute to the development and maintenance of IBD. Regulation of their common upstream signaling, that is, reactive oxygen species (ROS), may be important to control the progression of IBD. In the present study, we found that procyanidin, a powerful antioxidation flavonoid, has a significant effect on ROS clearance on THP-1 macrophages after lipopolysaccharide (LPS) or LPS-combined adenosine triphosphate stimulation, thus downregulating MMP9 expression, suppressing NF-κB signaling, and interrupting the formation of the NLRP3 inflammasome. Moreover, our in vivo data showed that procyanidin attenuated Dextran sulfate sodium-induced experimental colitis in a dose-dependent fashion by suppressing the expression of MMP9, NF-κB, and NLRP3 inflammasome signaling in colonic tissues in mice. Overall, our results suggested that targeting ROS could be a potential therapeutic choice for colonic inflammation.

CAS / MDL: 20347-71-1
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Food & Function · 2019 ·Vol. 10 ·期 2 ·765-774 · IF 3.241

Protein–polyphenol interactions enhance the antioxidant capacity of phenolics: analysis of rice glutelin–procyanidin dimer interactions

Taotao Dai,Jun Chen,David Julian McClements,Peng Hu,Xiaoqin Ye,Chengmei Liu,Ti Li

Rice glutelin and procyanidins are often used in functional foods as sources of plant-based proteins and polyphenols, respectively, but little is currently known about the interactions between them. In our research, the interaction between rice glutelin and the B-type procyanidin dimer (PB2) was investigated. The presence of the PB2 decreased the α-helix and random coil structure of the rice protein and reduced its surface hydrophobicity. However, the PB2 did not adversely affect the functional performance of RG in emulsions. Conversely, the antioxidant capacity of the PB2 was enhanced in the presence of the rice protein. Fluorescence spectroscopy confirmed that the protein and PB2 formed molecular complexes, which were primarily the result of hydrophobic attractive forces. Molecular docking analysis provides insights into the nature of the interaction between the rice protein and PB2. This study provides valuable insights into the nature of the interactions between plant proteins and polyphenolic nutraceuticals.

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ACS Applied Materials & Interfaces · 2014 · IF 5.9

Facile in Situ Synthesis of Silver Nanoparticles on Procyanidin-Grafted Eggshell Membrane and Their Catalytic Properties

Miao Liang,Rongxin Su,Renliang Huang,Wei Qi,Yanjun Yu,Libing Wang,Zhimin He

Facile, efficient, and robust immobilization of metal nanostructures on porous bioscaffolds is an interesting topic in materials chemistry and heterogeneous catalysis. This study reports a facile in situ method for the synthesis and immobilization of small silver nanoparticles (AgNPs) at room temperature on natural eggshell membrane (ESM), which presents interwoven fibrous structure and can be used as a unique protein-based biotemplate. Procyanidin (Pro), a typical plant polyphenol extracted from grape seeds and skins, was first grafted onto ESM fibers to serve as both reductant and stabilizer during the synthesis process. As a result, the AgNPs were facilely synthesized and robustly immobilized on the ESM fibers without additional chemical reductant or physical treatments. The morphology and microstructure of the as-prepared AgNPs@Pro-ESM composites were characterized by combined microscopy and spectroscopy technologies. The results indicate that small AgNPs with mean diameter of 2.46 nm were successfully prepared on the Pro-ESM biotemplate. The composites exhibited good catalytic activity toward the reduction of 4-nitrophenol (4-NP). More importantly, these composite catalysts can be easily recovered and reused for more than eight cycles because of their high stability.

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