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  • Brand : BIOFRON

  • Catalogue Number : BF-P2006

  • Specification : 98%

  • CAS number : 81-54-9

  • Formula : C14H8O5

  • Molecular Weight : 256.21

  • PUBCHEM ID : 6683

  • Volume : 20mg

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Catalogue Number


Analysis Method






Molecular Weight



Orange-Red crystalline powder

Botanical Source

Rubia cordifolia

Structure Type



Standards;Natural Pytochemical;API




Verantin/Purpurin/1,2,4-Trihydroxy-9,10-anthracenedione/C.I. Natural Red 16/natural red 16/1,2,4-Trihydroxy-9,10-anthraquinone/9,10-Anthracenedione, 1,2,4-trihydroxy-/Purpurine/C.I. Natural Red 8/1,2,4-trihydroxyanthracene-9,10-dione/1,2,4-trishydroxy-9,10-anthraquinone/1,2,4-Trihydroxyanthraquinone/Smoke Brown G/Hydroxylizaric acid




1.7±0.1 g/cm3


Methanol; DMSO

Flash Point

285.4±25.2 °C

Boiling Point

525.1±45.0 °C at 760 mmHg

Melting Point



InChl Key

WGK Germany


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#:81-54-9) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate




The body responds to overnutrition by converting stem cells to adipocytes. In vitro and in vivo studies have shown polyphenols and other natural compounds to be anti-adipogenic, presumably due in part to their antioxidant properties. Purpurin is a highly antioxidative anthraquinone and previous studies on anthraquinones have reported numerous biological activities in cells and animals. Anthraquinones have also been used to stimulate osteoblast differentiation, an inversely-related process to that of adipocyte differentiation. We propose that due to its high antioxidative properties, purpurin administration might attenuate adipogenesis in cells and in mice.

Our study will test the effect purpurin has on adipogenesis using both in vitro and in vivo models. The in vitro model consists of tracking with various biomarkers, the differentiation of pre-adipocyte to adipocytes in cell culture. The compound will then be tested in mice fed a high-fat diet. Murine 3T3-L1 preadipocyte cells were stimulated to differentiate in the presence or absence of purpurin. The following cellular parameters were measured: intracellular reactive oxygen species (ROS), membrane potential of the mitochondria, ATP production, activation of AMPK (adenosine 5′-monophosphate-activated protein kinase), insulin-induced lipid accumulation, triglyceride accumulation, and expression of PPARγ (peroxisome proliferator activated receptor-γ) and C/EBPα (CCAAT enhancer binding protein α). In vivo, mice were fed high fat diets supplemented with various levels of purpurin. Data collected from the animals included anthropometric data, glucose tolerance test results, and postmortem plasma glucose, lipid levels, and organ examinations.

The administration of purpurin at 50 and 100 μM in 3T3-L1 cells, and at 40 and 80 mg/kg in mice proved to be a sensitive range: the lower concentrations affected several measured parameters, whereas at the higher doses purpurin consistently mitigated biomarkers associated with adipogenesis, and weight gain in mice. Purpurin appears to be an effective antiadipogenic compound.

The anthraquinone purpurin has potent in vitro anti-adipogenic effects in cells and in vivo anti-obesity effects in mice consuming a high-fat diet. Differentiation of 3T3-L1 cells was dose-dependently inhibited by purpurin, apparently by AMPK activation. Mice on a high-fat diet experienced a dose-dependent reduction in induced weight gain of up to 55%.


Adipogenesis; Anthraquinone; Antioxidant; Cell differentiation; Lipogenic diet; Madder; Mitochondria; Obesity; Rubia cordifolia


Anti-adipogenic and anti-obesity activities of purpurin in 3T3-L1 preadipocyte cells and in mice fed a high-fat diet.


Nam W1, Nam SH1, Kim SP2,3, Levin C4, Friedman M5.

Publish date

2019 Dec 11




Ribonucleoprotein (RNP) complexes and RNA-processing enzymes are attractive targets for antibiotic development owing to their central roles in microbial physiology. For many of these complexes, comprehensive strategies to identify inhibitors are either lacking or suffer from substantial technical limitations. Here, we describe an activity-binding-structure platform for bacterial ribonuclease P (RNase P), an essential RNP ribozyme involved in 5′ tRNA processing. A novel, real-time fluorescence-based assay was used to monitor RNase P activity and rapidly identify inhibitors using a mini-helix and a pre-tRNA-like bipartite substrate. Using the mini-helix substrate, we screened a library comprising 2560 compounds. Initial hits were then validated using pre-tRNA and the pre-tRNA-like substrate, which ultimately verified four compounds as inhibitors. Biolayer interferometry-based binding assays and molecular dynamics simulations were then used to characterize the interactions between each validated inhibitor and the P protein, P RNA and pre-tRNA. X-ray crystallographic studies subsequently elucidated the structure of the P protein bound to the most promising hit, purpurin, and revealed how this inhibitor adversely affects tRNA 5′ leader binding. This integrated platform affords improved structure-function studies of RNA processing enzymes and facilitates the discovery of novel regulators or inhibitors.

© The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.


A screening platform to monitor RNA processing and protein-RNA interactions in ribonuclease P uncovers a small molecule inhibitor.


Madrigal-Carrillo EA1, Diaz-Tufinio CA1,2, Santamaria-Suarez HA1, Arciniega M1, Torres-Larios A1.

Publish date

2019 Jul 9




Rubia cordifolia L., is an industrially viable medicinal crop and is widely exploited for the therapeutic potential of its bioactive metabolite, purpurin. The present investigation aimed to explore the chemotypic and molecular variability in seven wild populations of R. cordifolia from South Eastern Ghats region of India. Thirty-eight individuals were assessed for molecular fingerprinting (ISSR markers) and densitometric quantification of purpurin and alizarin. The populations of Yelagiri Hills and Shervaroy Hills contained the highest levels of alizarin (0.115 and 0.093%, respectively) while Pachamalai and Kolli Hills revealed the highest purpurin content (0.284 and 0.280%, respectively). Genetic diversity was generally higher in the same populations that produced higher metabolite content, with the exception of Pachamalai, suggesting a highly prioritized conservation concern. The study revealed a Nei’s total gene diversity at species level of 0.266 and of 0.187 at population level, with an average population genetic differentiation of 0.28. No clear genetic or chemical structure was retrieved between the studied populations, with individuals from different locations clustering together, and no significant correlation was obtained between metabolites and genetic diversity or between these and the populations’ geographic distances.


Eastern Ghats; HPTLC; Hierarchical clustering; Multivariate analysis; Population genetics; Rubia cordifolia L.


ISSR Characterization and Quantification of Purpurin and Alizarin in Rubia cordifolia L. Populations from India.


Natarajan S1, Mishra P2, Vadivel M1, Basha MG1, Kumar A2, Velusamy S3.

Publish date

2019 Feb

Description :

Purpurin inhibits adipocyte-derived leucine aminopeptidase and angiogenesis in a zebrafish model. PUMID/DOI:24928393 Biochem Biophys Res Commun. 2014 Jul 18;450(1):561-7. A natural product Purpurin was identified as one of the most potent inhibitors of A-LAP from the screening. In vitro enzymatic analyses showed that Purpurin inhibited A-LAP activity in a non-competitive manner with a Ki value of 20 M. In In addition, Purpurin showed a strong selectivity toward A-LAP versus another member of M1 family of zinc metallopeptidase, aminopeptidase N (APN). In angiogenesis assays, Purpurin inhibited the vascular endothelial growth factor (VEGF)-induced invasion and tube formation of human umbilical In addition, Purpurin inhibited in vivo angiogenesis in zebrafish embryo without toxicity. These data demonstrate that Purpurin is a novel specific inhibitor of A-LAP and could be developed as a new anti-angiogenic agent. Purpurin suppresses Candida albicans biofilm formation and hyphal development. PUMID/DOI:23226409 PLoS One. 2012;7(11):e50866 A striking and clinically relevant virulence trait of the human fungal pathogen Candida albicans is its ability to grow and switch reversibly among different morphological forms. Inhibition of yeast-to-hypha transition in C. albicans represents a new paradigm for antifungal intervention. We have previously demonstrated the novel antifungal activity of purpurin against Candida fungi. In this study, we extended our investigation by examining the in vitro effect of purpurin on C. albicans morphogenesis and biofilms. The susceptibility of C. albicans biofilms to purpurin was examined quantitatively by 2,3-bis(2-methoxy-4-nitro-5-sulfo-phenyl)-2H-tetrazolium-5-carboxanilide reduction assay. Hyphal formation and biofilm ultrastructure were examined qualitatively by scanning electron microscopy (SEM). Quantitative reverse transcription-PCR (qRT-PCR) was used to evaluate the expression of hypha-specific genes and hyphal regulator in purpurin-treated fungal cells. The results showed that, at sub-lethal concentration (3 μg/ml), purpurin blocked the yeast-to-hypha transition under hypha-inducing conditions. Purpurin also inhibited C. albicans biofilm formation and reduced the metabolic activity of mature biofilms in a concentration-dependent manner. SEM images showed that purpurin-treated C. albicans biofilms were scanty and exclusively consisted of aggregates of blastospores. qRT-PCR analyses indicated that purpurin downregulated the expression of hypha-specific genes (ALS3, ECE1, HWP1, HYR1) and the hyphal regulator RAS1. The data strongly suggested that purpurin suppressed C. albicans morphogenesis and caused distorted biofilm formation. By virtue of the ability to block these two virulence traits in C. albicans, purpurin may represent a potential candidate that deserves further investigations in the development of antifungal strategies against this notorious human fungal pathogen in vivo.