We Offer Worldwide Shipping
Login Wishlist

Carmoisine

$96

  • Brand : BIOFRON

  • Catalogue Number : BN-O1378

  • Specification : 98%(HPLC)

  • CAS number : 3567-69-9

  • Formula : C20H14N2O7S2.2Na

  • Molecular Weight : 504.42

  • PUBCHEM ID : 19118

  • Volume : 20mg

Available on backorder

Quantity
Checkout Bulk Order?

Catalogue Number

BN-O1378

Analysis Method

HPLC,NMR,MS

Specification

98%(HPLC)

Storage

2-8°C

Molecular Weight

504.42

Appearance

Botanical Source

Chemosynthesis

Structure Type

Category

Standards;Natural Pytochemical;API

SMILES

C1=CC=C2C(=C1)C(=CC=C2S(=O)(=O)[O-])N=NC3=C(C4=CC=CC=C4C(=C3)S(=O)(=O)[O-])O.[Na+].[Na+]

Synonyms

Disodium 4-hydroxy-3-((4-sulphonatonaphthyl)azo)naphthalenesulphonate/Carmoisine B/Disodium 4-hydroxy-3-[(E)-(4-sulfonato-1-naphthyl)diazenyl]-1-naphthalenesulfonate/Disodium 4-hydroxy-3-[(E)-(4-sulfonato-1-naphthyl)diazenyl]naphthalene-1-sulfonate/1-Naphthalenesulfonic acid, 4-hydroxy-3-[(E)-2-(4-sulfo-1-naphthalenyl)diazenyl]-, sodium salt (1:2)/disodium 4-hydroxy-3-[(E)-(4-sulfonato-1-naphthyl)azo]naphthalene-1-sulfonate/foodred5/4-hydroxy-3,4'-azo-bis-naphthalene-1-sulfonic acid,disodium-salt/red#14/Mordant Blue 79/Chromotrope FB/carmoisin/disodium 4-hydroxy-3-[(E)-(4-sulfonatonaphthalen-1-yl)diazenyl]naphthalene-1-sulfonate/AZORUBIN/Azorubine/Brilliant Crimson Red/E122/acidred2c/1-naphthalenesulfonic acid, 4-hydroxy-3-[(E)-(4-sulfo-1-naphthalenyl)azo]-, disodium salt/karmesin/Acid red 14/Carmoisine/ciacidred

IUPAC Name

disodium;4-hydroxy-3-[(4-sulfonatonaphthalen-1-yl)diazenyl]naphthalene-1-sulfonate

Density

Solubility

Flash Point

>225℃

Boiling Point

Melting Point

>300ºC

InChl

InChl Key

WGK Germany

RID/ADR

HS Code Reference

2942000000

Personal Projective Equipment

Correct Usage

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

Meta Tag

provides coniferyl ferulate(CAS#:3567-69-9) 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

28650022

Abstract

The binding of the common food colorant carmoisine and its inhibitory effect on amyloid fibrillation in lysozyme have been investigated. Since humans are increasingly exposed to various food colorants like carmoisine, such studies are highly relevant. In the presence of lysozyme, the carmoisine absorption spectrum exhibited hypochromic changes. The intrinsic fluorescence of lysozyme was also quenched on interaction. Time-resolved fluorescence results suggested that the binding mechanism involved ground state complexation. The binding was predominantly dominated by non-polyelectrolytic forces. The molecular distance between the donor (lysozyme) and the acceptor (carmoisine), calculated from FRET theory, was found to be 3.37 nm, indicating that carmoisine binds close to Trp-62/63 residues in the β-domain of the protein. Information on alterations in the microenvironment surrounding the Trp-residues was also obtained from synchronous fluorescence data. Carmoisine binding induced significant loss in the alpha helical organization of lysozyme. The binding, nevertheless, did not influence the thermal stability of lysozyme significantly. The binding reaction was exothermic and driven by large negative enthalpy and small but favourable entropic contributions. Thioflavin T assay, far-UV circular dichroism studies and AFM imaging profiles testified that carmoisine had a significant inhibitory effect on amyloid fibrillogenesis in lysozyme. Carmoisine also had a definitive defibrillating effect on existing fibrils. The results may provide new insights for designing new small molecule inhibitors for amyloid related diseases.

Title

Interaction and inhibitory influence of the azo dye carmoisine on lysozyme amyloid fibrillogenesis.

Author

Basu A1, Suresh Kumar G1.

Publish date

2017 Jul 25

PMID

27928889

Abstract

Since natural pigments are lost during the processing of beverages such as pomegranate juice, carmoisine, as an adulterant, is often added into the pure juice to improve color characteristics. In this study, molecularly imprinted polymers, as an adsorbent of carmoisine, were synthesized using acrylamide, methacrylic acid, and 4-vinylpyridine as functional monomers and then they were evaluated in terms of the separation and detection of carmoisine. Experiments on the batch adsorption of carmoisine 10 ppm stock solution revealed a better binding capacity for the 4-vinylpyridine-based polymer in comparison to methacrylic acid and acrylamide polymers. The complexation of carmoisine with the 4-vinylpyridine-based polymer was confirmed by Fourier transform infrared spectroscopy. The synthesized polymer exerted a high thermal degradation point and average diameter of polymer particles were obtained to be 0.2 μm by dynamic light scattering analysis. This work showed that detection of pomegranate juice adulteration with carmoisine is not necessarily difficult, time consuming or expensive with selective separation techniques such as molecularly imprinted polymers.

© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

KEYWORDS

4-vinylpyridine; carmoisine; molecularly imprinted polymers; pomegranate juice

Title

Synthesis of a molecularly imprinted polymer for the selective recognition of carmoisine (Azorubin E122) from pomegranate juice.

Author

Ghasempour Z1, Alizadeh-Khaledabad M1, Vardast MR2, Rezazad-Bari M1.

Publish date

2017 Feb

PMID

28524270

Abstract

In this study, the interaction between human serum albumin (HSA) and a copper complex of carmoisine dye; [Cu(carmoisine)2 (H2 O)2 ], was studied in vitro using multi-spectroscopic methods. It was found that the intrinsic fluorescence of HSA was quenched by the addition of the [Cu(carmoisine)2 (H2 O)2 ] complex and the quenching mechanism was considered as static quenching by formation of a [Cu(carmoisine)2 (H2 O)2 ]-HSA complex. The binding constant was about 104 M-1 at room temperature. The values of the calculated thermodynamic parameters (ΔH < 0 and ΔS > 0) suggested that both hydrogen bonds and the hydrophobic interactions were involved in the binding process. The site marker competitive experiments revealed that the binding of [Cu(carmoisine)2 (H2 O)2 ] to HSA primarily occurred in subdomain IIIA (site II) of HSA. The results of circular dichroism (CD) and UV-vis spectroscopy showed that the micro-environment of amino acid residues and the conformation of HSA were changed after addition of the [Cu(carmoisine)2 (H2 O)2 ] complex. Finally, the binding of the [Cu(carmoisine)2 (H2 O)2 ] complex to HSA was modelled by a molecular docking method. Excellent agreement was obtained between the experimental and theoretical results with respect to the binding forces and binding constant.

Copyright © 2017 John Wiley & Sons, Ltd.

KEYWORDS

carmoisine dye; copper(II) complex; fluorescence spectroscopy; human serum albumin (HSA)

Title

Interaction studies of copper complex containing food additive carmoisine dye with human serum albumin (HSA): Spectroscopic investigations.

Author

Shahabadi N1,2, Akbari A3, Jamshidbeigi M3, Fili SM1.

Publish date

2017 Nov


Description :

Empty ...