• Chemistry, Medicine
• Published in Food chemistry 2013
• DOI:10.1016/j.foodchem.2013.05.026

Interaction of anthocyanins with human serum albumin: influence of pH and chemical structure on binding.

@article{Cahyana2013InteractionOA,
  title={Interaction of anthocyanins with human serum albumin: influence of pH and chemical structure on binding.},
  author={Yana Cahyana and Michael L. Gordon},
  journal={Food chemistry},
  year={2013},
  volume={141 3},
  pages={
          2278-85
        }
}

• Yana Cahyana, Michael L. Gordon

The affinity of anthocyanins for human serum albumin (HSA) was determined by a fluorescence quenching method. The effects of pH and structure of anthocyanins on the binding constants were studied. The constants for binding of anthocyanins to HSA ranged from 1.08×10(5) to 13.2×10(5) M(-1). A hydrophobic effect at acidic pH was shown by the relatively high positive entropy values under the conditions studied. Electrostatic interactions, including hydrogen bonding, contributed to the binding at pH… CONTINUE READING

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