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Karanjin

$560

  • Brand : BIOFRON

  • Catalogue Number : BD-P0807

  • Specification : 98.5%(HPLC&TLC)

  • CAS number : 521-88-0

  • PUBCHEM ID : 100633

  • Volume : 25mg

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Catalogue Number

BD-P0807

Analysis Method

HPLC,NMR,MS

Specification

98.5%(HPLC&TLC)

Storage

2-8°C

Molecular Weight

Appearance

Acicular crystal

Botanical Source

Pongamia pinnata (L.) Pierre

Structure Type

Flavonols/Flavanonols

Category

Standards;Natural Pytochemical;API

SMILES

COC1=C(OC2=C(C1=O)C=CC3=C2C=CO3)C4=CC=CC=C4

Synonyms

Karanjin/4H-Furo[2,3-h]-1-benzopyran-4-one, 3-methoxy-2-phenyl-/3-Methoxy-2-phenyl-4H-furo[2,3-h]-1-benzopyran-4-one/3-Methoxy-2-phenyl-4H-furo[2,3-h]chromen-4-one/3-methoxy-2-phenylfuro[2,3-h]chromen-4-one/3-Methoxy-2-phenyl-4H-furo(2,3-h)(1)benzopyran-4-one

IUPAC Name

3-methoxy-2-phenylfuro[2,3-h]chromen-4-one

Applications

Density

1.4±0.1 g/cm3

Solubility

Methanol; Acetontrile; DMSO

Flash Point

233.8±28.7 °C

Boiling Point

463.0±45.0 °C at 760 mmHg

Melting Point

156ºC

InChl

InChl Key

WGK Germany

RID/ADR

HS Code Reference

2932990000

Personal Projective Equipment

Correct Usage

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

Meta Tag

provides coniferyl ferulate(CAS#:521-88-0) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate

No Technical Documents Available For This Product.

PMID

28706329

Abstract

OBJECTIVES:
The objective of this study is to evaluate the beneficial effect of karanjin for the treatment of experimental colitis.

METHODS:
Colitis was induced in the Balb/c mice by rectal administration of 2% solution of 2,4,6-trinitrobenzenesulfonic acid (TNBS) in 50% methanol. Karanjin (>98% pure) was administered in two different concentrations 100 and 200 mg/kg and sulfasalazine (100 mg/kg) as reference for 7 consecutive days to colitic mice. On the 8 day, mice were euthanized and degree of inflammation was assessed by macroscopic, microscopic, histology and biochemical estimation of myeloperoxidase (MPO), nitric oxide (NO), malondialdehyde (MDA), catalase (CAT), superoxide dismutase (SOD), and reduced glutathione (GSH) level were measured.

RESULTS:
Karanjin significantly and dose dependently ameliorate the macroscopic damage, histological changes such as cellular infiltration, tissue necrosis, mucosal and submucosal damage as compared to the TNBS control group. Karanjin reduces the activity of MPO, depressed MDA, and NO level and helps in restoring the level of CAT, SOD, and GSH to normal when compared to the TNBS colitis group.

CONCLUSION:
Result of the present study indicates that karanjin has the potential to cure colitis induced by intracolonic administration of TNBS.

KEYWORDS

2,4,6-trinitrobenzenesulfonic acid induced colitis; Pongamia pinnata; furanoflavonoid; inflammatory bowel diseases; karanjin

Title

Effect of karanjin on 2,4,6-trinitrobenzenesulfonic acid-induced colitis in Balb/c mice.

Author

Patel PP1, Trivedi ND2.

Publish date

2017 Mar-Apr

PMID

31153458

Abstract

Karanjin, a furanoflavonol from Pongamia pinnata L is used in agricultural practices for its pesticidal, insecticidal and acaricidal activities. It is commercially available as a bio-pesticide targeting a wide variety of pests. The present study was intended to evaluate the biochemical interactions of karanjin with bovine serum albumin (BSA) and study its toxicological effects on mammalian and bacterial cell lines. Karanjin bound to BSA at a single site with a dissociation constant of 19.7 μM. Evaluation of BSA-karanjin interactions at three different temperatures indicated the involvement of static mode of quenching. Binding experiments in the presence of warfarin and computational docking analysis indicated that karanjin bound closer to the warfarin binding site located in the Subdomain IIA of BSA. Using Forster resonance energy transfer analysis the distance between TRP 213 of BSA and karanjin was found to be 20 a. Collective results from synchronous fluorescence spectra analysis, differential scanning calorimetry, and circular dichroism analysis indicated that binding of karanjin induced conformational changes in the secondary structure of BSA. Karanjin exhibited low toxicity against human cervical cancer cells and normal mouse fibroblast L929 cells and modestly inhibited the growth of B. subtilis and E. coli cells. The data presented in this study provides insights for understanding the binding interactions of karanjin with BSA and its possible toxicological effects on mammalian cell lines and bacteria.

Copyright © 2019 Elsevier Inc. All rights reserved.

KEYWORDS

Bio-pesticide; Bovine serum albumin; Cytotoxicity and computational docking; Forster resonance energy transfer; Karanjin

Title

Biochemical and toxicological investigation of karanjin, a bio-pesticide isolated from Pongamia seed oil.

Author

Raghav D1, Mahanty S1, Rathinasamy K2.

Publish date

2019 Jun

PMID

30108931

Abstract

CYP1A1 is thought to mediate carcinogenesis in oral, lung and epithelial cancers. In order to identify a CYP1A1 inhibitor from an edible plant, 394 natural products in the IIIM’s natural product repository were screened, at 10 μM concentration, using CYP1A1-Sacchrosomes™ (i.e. microsomal enzyme isolated from recombinant baker’s yeast). Twenty-seven natural products were identified that inhibited 40-97% of CYP1A1’s 7-ethoxyresorufin-O-deethylase activity. The IC50 values of the ‘hits’, belonging to different chemical scaffolds, were determined. Their selectivity was studied against a panel of 8 CYP-Sacchrosomes™. In order to assess cellular efficacy, the ‘hits’ were screened for their capability to inhibit CYP enzymes expressed within live recombinant human embryonic kidney (HEK293) cells from plasmids encoding specific CYP genes (1A2, 1B1, 2C9, 2C19, 2D6, 3A4). Isopimpinellin (IN-475; IC50, 20 nM) and karanjin (IN-195; IC50, 30 nM) showed the most potent inhibition of CYP1A1 in human cells. Isopimpinellin is found in celery, parsnip, fruits and in the rind and pulp of limes whereas different parts of the Indian beech tree, which contain karanjin, have been used in traditional medicine. Both isopimpinellin and karanjin negate the cellular toxicity of CYP1A1-mediated benzo[a]pyrene. Molecular docking and molecular dynamic simulations with CYP isoforms rationalize the observed trends in the potency and selectivity of isopimpinellin and karanjin.

Title

Identification of karanjin isolated from the Indian beech tree as a potent CYP1 enzyme inhibitor with cellular efficacy via screening of a natural product repository.

Author

Joshi P1,2, Sonawane VR3, Williams IS3,4, McCann GJP3, Gatchie L3,4, Sharma R2,5, Satti N5, Chaudhuri B3, Bharate SB1,2.

Publish date

Joshi P1,2, Sonawane VR3, Williams IS3,4, McCann GJP3, Gatchie L3,4, Sharma R2,5, Satti N5, Chaudhuri B3, Bharate SB1,2.