Study on the interaction of artificial and natural food colorants with human serum albumin: A computational point of view

Comput Biol Chem. 2015 Jun;56:152-8. doi: 10.1016/j.compbiolchem.2015.04.006. Epub 2015 Apr 20.


Due to the high amount of artificial food colorants present in infants' diets, their adverse effects have been of major concern among the literature. Artificial food colorants have been suggested to affect children's behavior, being hyperactivity the most common disorder. In this study we compare binding affinities of a group of artificial colorants (sunset yellow, quinoline yellow, carmoisine, allura red and tartrazine) and their natural industrial equivalents (carminic acid, curcumin, peonidin-3-glucoside, cyanidin-3-glucoside) to human serum albumin (HSA) by a docking approach and further refinement through atomistic molecular dynamics simulations. Due to the protein-ligand conformational interface complexity, we used collective variable driven molecular dynamics to refine docking predictions and to score them according to a hydrogen-bond criterion. With this protocol, we were able to rank ligand affinities to HSA and to compare between the studied natural and artificial food additives. Our results show that the five artificial colorants studied bind better to HSA than their equivalent natural options, in terms of their H-bonding network, supporting the hypothesis of their potential risk to human health.

Keywords: Docking; Food colorants; Human serum albumin; Molecular dynamics.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biological Products / chemistry
  • Biological Products / metabolism
  • Food Coloring Agents / chemistry
  • Food Coloring Agents / metabolism*
  • Humans
  • Hydrogen Bonding
  • Infant
  • Molecular Docking Simulation
  • Molecular Dynamics Simulation
  • Protein Binding
  • Serum Albumin / chemistry
  • Serum Albumin / metabolism*


  • Biological Products
  • Food Coloring Agents
  • Serum Albumin