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20S-Protopanaxatriol

$85

  • Brand : BIOFRON

  • Catalogue Number : BF-P1013

  • Specification : 98%

  • CAS number : 34080-08-5

  • Formula : C30H52O4

  • Molecular Weight : 476.73

  • Volume : 20mg

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Catalogue Number

BF-P1013

Analysis Method

HPLC,NMR,MS

Specification

98%

Storage

2-8°C

Molecular Weight

476.73

Appearance

Botanical Source

Panax ginseng

Structure Type

Triterpenoids

Category

SMILES

CC(=CCCC(C)(C1CCC2(C1C(CC3C2(CC(C4C3(CCC(C4(C)C)O)C)O)C)O)C)O)C

Synonyms

IUPAC Name

Applications

Density

1.1±0.1 g/cm3

Solubility

DMSO : ≥ 47 mg/mL (98.59 mM)
*"≥" means soluble, but saturation unknown.

Flash Point

242.9±24.7 °C

Boiling Point

588.8±50.0 °C at 760 mmHg

Melting Point

InChl

InChI=1S/C30H52O4/c1-18(2)10-9-13-30(8,34)19-11-15-28(6)24(19)20(31)16-22-27(5)14-12-23(33)26(3,4)25(27)21(32)17-29(22,28)7/h10,19-25,31-34H,9,11-17H2,1-8H3/t19-,20+,21-,22+,23-,24-,25-,27+,28+,29+,30-/m0/s1

InChl Key

SHCBCKBYTHZQGZ-PHFGEWBZSA-N

WGK Germany

RID/ADR

HS Code Reference

Personal Projective Equipment

Correct Usage

For Reference Standard and R&D, Not for Human Use Directly.

Meta Tag

provides coniferyl ferulate(CAS#:34080-08-5) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate

PMID

31671229

Abstract

Noncovalent interactions between drugs and proteins play significant roles for drug metabolisms and drug discoveries. Mass spectrometry has been a commonly used method for studying noncovalent interactions. However, the harsh ionization process in electrospray ionization mass spectrometry (ESI-MS) is not conducive to the preservation of noncovalent and unstable biomolecular complexes compared with the cold spray ionization mass spectrometry (CSI-MS). A cold spray ionization providing a stable solvation-ionization at low temperature is milder than ESI, which was more suitable for studying noncovalent drug-protein complexes with exact stoichiometries. In this paper, we apply CSI-MS to explore the interactions of ginsenosides toward amyloid-β-peptide (Aβ) and clarify the therapeutic effect of ginsenosides on Alzheimer’s disease (AD) at the molecular level for the first time. The interactions of ginsenosides with Aβ were performed by CSI-MS and ESI-MS, respectively. The ginsenosides Rg1 bounded to Aβ at the stoichiometries of 1:1 to 5:1 could be characterized by CSI-MS, while dehydration products are more readily available by ESI-MS. The binding force depends on the number of glycosyls and the type of ginsenosides. The relative binding affinities were sorted in order as follows: Rg1 ? Re > Rd ? Rg2 > Rh2, protopanaxatriol by competition experiments, which were supported by molecular docking experiment. CSI-MS is expected to be a more appropriate approach to determine the weak but specific interactions of proteins with other natural products especially polyhydroxy compounds.

KEYWORDS

amyloid-β-peptide; cold spray ionization; ginsenosides; mass spectrometry; noncovalent interactions

Title

Study of the noncovalent interactions of ginsenosides and amyloid-β-peptide by CSI-MS and molecular docking

Author

Yanan Zhou 1, Su Chen 1, Jinping Qiao 2, Yanyun Cui 2 3, Chang Yuan 2, Lan He 1, Jin Ouyang 2

Publish date

2020 Jan;

PMID

31454649

Abstract

Background: P2Y12 receptor (P2Y12R) is a newly discovered Gi-coupled ADP receptor that plays critical role in platelet function. Ginsenosides are the main constituents responsible for most of pharmacological actions of ginseng, especially cardio-cerebrovascular protective efficacy that is closely related to the influence on platelet function.

Hypothesis/purpose: To explore stereoselective effect of naturally abundant ginsenoside isomers, including the C-20 epimers of protopanaxadiol (PPD), protopanaxatriol (PPT), and their glycosides Rg2, Rg3, Rh1, Rh2 on P2Y12R in platelets.

Study design/methods: Both in vitro assay and in silico molecular docking study were performed to investigate the stereoselective effects.

Results: In vitro assay using washed rat platelets revealed differential effects of ginsenoside isomers on ADP-induced platelet aggregation with the direction and degree of action varying with chemical structures. More to the point, the ginsenoside 20S-Rh2 but not its 20R-epimer was found to be the only one that could significantly promote in vitro platelets aggregation induced by ADP. The correlation analysis demonstrated that ginsenosides may have impact on P2Y12R related platelet functions through a cAMP-dependent pathway. Molecular docking stimulation further indicated that ginsenoside isomers could be potent substrate of P2Y12R with differential protein-ligand interaction that would be responsible for the stereoselective efficacy of C-20 ginsenoside epimers. Hydrogen bonding with Asp266 via the C-20 hydroxyl may provide ginsenosides with promoting effect on ADP-induced platelets aggregation, whereas interactions with Tyr105 could contribute to the promotion of inhibitory efficacy.

Conclusion: Ginsenosides are potent P2Y12R substrate with stereoselective effects on P2Y12R-related platelet function, which result from their chemical diversity and are closely related to the different interaction ways as P2Y12R ligand.

KEYWORDS

Ginsenoside C-20 isomers; Ligand-receptor interaction; P2Y(12) receptor; Platelet aggregation; Stereoselective effects.

Title

In vitro and in silico evaluation of stereoselective effect of ginsenoside isomers on platelet P2Y 12 receptor

Author

Qianwen Yang 1, Ning Wang 1, Jie Zhang 1, Geng Chen 2, Hui Xu 3, Qingguo Meng 4, Yuan Du 1, Xin Yang 2, Huaying Fan 1

Publish date

2019 Nov

PMID

31289903

Abstract

Use of recombinant glycosidases is a promising approach for the production of minor ginsenosides, e.g., Compound K (CK) and F1, which have potential applications in the food industry. However, application of these recombinant enzymes for food-grade preparation of minor ginsenosides are limited by the lack of suitable expression hosts and low productivity. In this study, Corynebacterium glutamicum ATCC13032, a GRAS strain that has been used extensively for the industrial-grade production of additives for foodstuffs, was employed to express a novel β-glucosidase (MT619) from Microbacterium testaceum ATCC 15829 with high ginsenoside-transforming activity. A cellulose-binding module was additionally fused to the N-terminus of MT619 for immobilization on cellulose, which is an abundant and safe material. Via one-step immobilization, the fusion protein in cell lysates was efficiently immobilized on regenerated amorphous cellulose at a high density (maximum 984 mg/g cellulose), increasing the enzyme concentration by 286-fold. The concentrated and immobilized enzyme showed strong conversion activities against protopanaxadiol- and protopanaxatriol-type ginsenosides for the production of CK and F1. Using gram-scale ginseng extracts as substrates, the immobilized enzyme produced 7.59 g/L CK and 9.42 g/L F1 in 24 h. To the best of our knowledge, these are the highest reported product concentrations of CK and F1, and this is the first time that a recombinant enzyme has been immobilized on cellulose for the preparation of minor ginsenosides. This safe, convenient, and efficient production method could also be effectively exploited in the preparation of food-processing recombinant enzymes in the pharmaceutical, functional food, and cosmetics industries.

KEYWORDS

Biotransformation; Compound K; Corynebacterium glutamicum; Deglycosylation; Ginsenoside F1.

Title

High-density immobilization of a ginsenoside-transforming β-glucosidase for enhanced food-grade production of minor ginsenosides

Author

Chang-Hao Cui 1 2, Byeong-Min Jeon 3, Yaoyao Fu 2, Wan-Taek Im 4, Sun-Chang Kim 5 6 7

Publish date

2019 Sep;