Adverse reactions to food additives

MacGibbon, B.H.

doi:10.1079/pns19830027

Cited by 4 publications

(1 citation statement)

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“…ErB was also recently also shown to cause genotoxicity at concentrations ≥50 μM using a hepatocellular carcinoma HepG2 cell line (Chequer et al ., ). Hence, an obvious concern related to this promiscuous inhibitory activity is the possibility of toxic side effects in humans, especially as a number of possible behavioral alterations and food allergies have been often – and controversially – linked to food colorants (MacGibbon, ), and this is likely to become an increasingly important issue because, for example, in the US, the use of food dyes increased about fivefold since 1955 and currently about 100 t of ErB are produced annually and certified by the FDA (Kobylewski and Jacobson, ). The current acceptable daily intake (ADI) for ErB is 0.1 mg/kg body weight/day (Gardner et al ., ; JECFA, ; EFSA, ), already considerably lower than that of any other FDA‐approved food color (e.g., 7 mg/kg body weight/day for allura red or 7.5 for tartrazine; Glória, ).…”

Section: Discussionmentioning

confidence: 99%

The promiscuous protein binding ability of erythrosine B studied by metachromasy (metachromasia)

Ganesan

Buchwald

2013

J of Molecular Recognition

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The present study aims to elucidate aspects of the protein binding ability of erythrosine B (ErB), a poly-iodinated xanthene dye and an FDA-approved food colorant (FD&C Red No. 3), which we have identified recently as a promiscuous inhibitor of protein–protein interactions (PPI) with a remarkably consistent median inhibitory concentration (IC50) in the 5–30 µM range. Because ErB exhibits metachromasy, i.e., color change upon binding to several proteins, we exploited this property to quantify its binding to proteins such as bovine serum albumin (BSA) and CD40L (CD154) and to determine the corresponding binding constants (Kd) and stoichiometry (nb) using spectrophotometric methods. Binding was reversible and the estimated affinities for both protein targets obtained here (Kd values of 14 and 20 µM for BSA and CD40L, respectively) were in good agreement with that expected from the protein–protein interaction (PPI) inhibitory activity of ErB. A stoichiometry greater than one was observed both for CD40L and BSA binding (nb of 5–6 and 8–9 for BSA and CD40L, respectively) indicating the possibility of nonspecific binding of the flat an rigid ErB molecule at multiple sites, which could explain the promiscuous PPI inhibitory activity if some of these overlap with the binding site of the protein partner and interfere with the binding.

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Section: Discussionmentioning

confidence: 99%