FOOD CHEMISTRY
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2018
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IF 4.946
Hui Cao,Xiaojuan Liu,Nataša Poklar Ulrih,Pradeep K. Sengupta,Jianbo Xiao
Herein, the protein binding rates of structurally different flavonoids to human serum albumin (HSA) were elucidated by applying the high performance affinity chromatography (HPAC). The flavonoids with hydroxyl groups on ring A showed a higher protein binding rate compared with those that there was no hydroxyl on ring A. However, the hydroxylation of ring B lowered the protein binding rate. It was also found that an additional methoxy group in flavone ring A would decrease the protein binding rate. Nevertheless, the methoxy group in flavanone ring A (position 6) and isoflavone ring B (position 4′) increased the protein binding rate. Methoxy group at other positions of flavonoids slightly enhanced or no significantly affected the binding rates on human serum albumin. Hydrogenation of C2 C3 double bond of flavonoids decreased the protein binding rate and had the same effect as glycosylation which decrease the protein binding rate by 5%–25%.
研究领域:
药理学
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生物化学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
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2024
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IF 4.3
Hongxin Tan,Yi Zhao,Xiuqin Zhang,Haitao Ma,Hongyan Zhang
The use of fluorescent carbon dots (CDs) as highly precise biolabeling probes has been widespread in the fields of live cell imaging and protein labeling due to their small size and excellent photoluminescence ability to accurately target specific molecules with surface chemical properties. However, there was a lack of research on the interaction between CDs and labeled molecules. In this work, we presented a novel investigation strategy, the fluorescence microscopy-surface plasmon resonance (FM-SPR) system, which combined the use of fluorescence microscopy and wavelength modulation surface plasmon resonance to study the interaction between CDs and labeled molecules in real-time. Using this system, simultaneously recorded the SPR signals and the fluorescence images on the surface of the FM-SPR sensor chip. We observed the dynamic curve and fluorescence images of the interaction between green emissive nitrogen-doped carbon dots (N-CDs) and silk fibroin (SF) in real-time. The kinetic parameters, the quantitative analysis, and the investigation of the binding could be achieved. The results showed a strong linear relationship between the change in SPR signals and the concentration of N-CDs, with a linear coefficient of 0.99913. The linear detection range was 2.5 μg/mL–100 μg/mL, and the real lowest detection limit reached 0.5 μg/mL. Additionally, the green fluorescence points in the imaging region on the FM-SPR sensor chip increased with the concentration of N-CDs, which was consistent with the change in SPR signals. Using this system we also acquired the association rate and dissociation rate of N-CDs to SF which were 2.65 × 10 −5 /s and 1.52 × 10 −5 /s, respectively. This demonstrated the effectiveness of our method in quantitatively analyzing SF labeled with N-CDs.
研究领域:
材料科学
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生物物理学
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分析化学
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生物化学
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产品关联
DOI
PubMed
高影响因子
JOURNAL OF ETHNOPHARMACOLOGY
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2024
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IF 4.8
Qiao-Lai Wang,Pei-Xi Zhang,Rui Shen,Meng Xu,Liang Han,Xuan Shi,Zi-Rui Zhou,Jing-Yi Yang,Jie-Qing Liu
Ethnopharmacological relevance Arbutin is a naturally occurring glucoside extracted from plants, known for its antioxidant and tyrosinase inhibiting properties. It is widely used in cosmetic and pharmaceutical industries. With in-depth study of arbutin, its application in disease treatment is expanding, presenting promising development prospects. However, reports on the metabolic stability, plasma protein binding rate, and pharmacokinetic properties of arbutin are scarce. Aim of the study The aim of this study is to enrich the data of metabolic stability and pharmacokinetics of arbutin through the early pre-clinical evaluation, thereby providing some experimental basis for advancing arbutin into clinical research. Materials and methods We developed an efficient and rapid liquid chromatography-tandem mass spectrometry (LC-MS/MS) assay for determining arbutin in plasma. We investigated the metabolic and pharmacokinetic properties of arbutin through in vitro metabolism assay, cytochrome enzymes P450 (CYP450) inhibition studies, plasma protein binding rate analysis, Caco-2 cell permeability tests, and rat pharmacokinetics to understand its in vivo performance. Results In vitro studies show that arbutin is stable, albeit with some species differences. It exhibits low plasma protein binding (35.35 ± 11.03% ∼ 40.25 ± 2.47%), low lipophilicity, low permeability, short half-life (0.42 ± 0.30 h) and high oral bioavailability (65 ± 11.6%). Arbutin is primarily found in the liver and kidneys and is eliminated in the urine. It does not significantly inhibit CYP450 up to 10 μM, suggesting a low potential for drug interactions. Futhermore, preliminary toxicological experiments indicate arbutin's safety, supporting its potential as a therapeutic agent. Conclusion This study provides a comprehensive analysis the drug metabolism and pharmacokinetics (DMPK) of arbutin, enriching our understanding of its metabolism stability and pharmacokinetics properties, It establishes a foundation for further structural optimization, pharmacological studies, and the clinical development of arbutin.
研究领域:
药理学
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分析化学
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临床前研究
✓ 已验证
产品关联
DOI
PubMed
高影响因子
LWT-FOOD SCIENCE AND TECHNOLOGY
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2024
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IF 6
Meiyu Gu,Jiahui Shi,Boya Zhang,Xibo Wang,Xu Wang
The effect of covalent binding of different concentrations of hydroxytyrosol (HT) to soy protein isolate (SPI) by enzymatic method on the structure and function of the complex was investigated. Polyphenol binding rate increased and then decreased with increasing hydroxytyrosol concentration, with a maximum binding rate of 38.10 ± 1.08%. Covalent binding to HT resulted in a significant increase in the turbidity of the adduct and a significant decrease in the free sulfhydryl content and surface hydrophobicity. The structure of the adduct was altered and the α-helix structure was converted to a β-sheet one. The maximum foaming property of the adducts was observed at a HT concentration of 40 μmol/g, which was 28.84% higher than the control SPI. The adduct had maximum solubility (52.84 ± 0.18%) at HT concentration of 50 μmol/g. The emulsifying properties of the adducts were maximized at a hydroxytyrosol concentration of 60 μmol/g. When the HT concentration was 70 μmol/g, the DPPH and ABTS radical scavenging rates of the adducts were increased by 245.03% and 26.35%, respectively, compared with the control SPI.
研究领域:
食品科学
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蛋白质化学
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生物技术
✓ 已验证
产品关联
DOI
高影响因子
危险品化学品经营许可证（带存储）