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Determination of meaty peptide in enzymatic hydrolyzate of beef protein by HPLC-MS
Yanping Wang,Songrong Zeng,Xiaojia Bai,Weili Lin,Ming Yang,Haipeng Xing 한국화학공학회 2008 Korean Journal of Chemical Engineering Vol.25 No.5
The purpose of this study is to detect beefy meaty peptide (BMP) in beef hydrolyzate. The synthesized BMP is used as a standard sample in the study. High performance liquid chromatography (HPLC)/ion trap electrospray ionization mass spectrometry (ESI-MS) with UV detection was applied in qualitative analysis of the peptides. Six beef protein enzymatic hydrolyzate samples were separated on a Surveyor HPLC system through a SUPELCO Discovery® C18 analytical column (5 μm, 15 cm×2.1 mm i.d.). The column was eluted at a flow rate of 0.2 mL/min in a linear gradient elution mode of acetronitrile-water solution with 0.1% trifluoroacetic acid. The concentration of acetronitrile was increased from 5% to 50% in 40 minutes. A Finnigan LCQ Advantage MAX instrument was used as detector to analyze with ESI-MS and ESI-MS/MS in positive mode. Among the six samples of beef protein enzymatic hydrolysate, the BMP is detected and confirmed in sample No.4 with a higher intensity of characteristic peak and is further investigated by ESI-MS/MS. As a result, BMP exists in sample No.4. The study proves that HPLC-ESI-MS/MS is a simple, rapid, sensitive method to analyze target peptides from complex polypeptides
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Tiehua Zhang,Shuning Zhong,Ligang Hou,Yongjun Wang,XiaoJia Xing,Tianzhu Guan,Jie Zhang,Tiezhu Li 고려인삼학회 2020 Journal of Ginseng Research Vol.44 No.5
Background: As the main metabolites of ginsenosides, 20(S, R)-protopanaxadiol [PPD(S, R)] and 20(S, R)-protopanaxatriol [PPT(S, R)] are the structural basis response to a series of pharmacological effects of their parent components. Although the estrogenicity of several ginsenosides has been confirmed, however, the underlying mechanisms of their estrogenic effects are still largely unclear. In this work, PPD(S, R) and PPT(S, R) were assessed for their ability to bind and activate human estrogen receptor α(hERα) by a combination of in vitro and in silico analysis. Methods: The recombinant hERα ligand-binding domain (hERa-LBD) was expressed in E. coli strain. The direct binding interactions of ginsenosides with hERα-LBD and their ERα agonistic potency were investigated by fluorescence polarization and reporter gene assays, respectively. Then, molecular dynamics simulations were carried out to simulate the binding modes between ginsenosides and hERα-LBD to reveal the structural basis for their agonist activities toward receptor. Results: Fluorescence polarization assay revealed that PPD(S, R) and PPT(S, R) could bind to hERα-LBD with moderate affinities. In the dual luciferase reporter assay using transiently transfected MCF-7 cells, PPD(S, R) and PPT(S, R) acted as agonists of hERα. Molecular docking results showed that these ginsenosides adopted an agonist conformation in the flexible hydrophobic ligand-binding pocket. The stereostructure of C-20 hydroxyl group and the presence of C-6 hydroxyl group exerted significant influence on the hydrogen bond network and steric hindrance, respectively. Conclusion: This work may provide insight into the chemical and pharmacological screening of novel therapeutic agents from ginsenosides.
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