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

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Cahyana, Y. and Gordon, M. H. (2013) Interaction of anthocyanins with human serum albumin: influence of pH and chemical structure on binding. Food Chemistry, 141 (3). pp. 2278-2285. ISSN 0308-8146

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To link to this item DOI: 10.1016/j.foodchem.2013.05.026

Abstract/Summary

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 x 10^5 M-1 to 13.16 x 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 7.4. The effect of structure of anthocyanins on the affinity was pH dependent, particularly the effect of additional hydroxyl substituents. Hydroxyl substituents and glycosylation of anthocyanins decreased the affinity for binding to HSA at lower pH (especially pH 4), but increased the strength of binding at pH 7.4. In contrast, methylation of a hydroxyl group enhanced the binding at acidic pH, while this substitution reduced the strength of binding at pH 7.4. This paper has shown that changes in anthocyanin structure or reductions in pH, which may occur in the region of inflammatory sites, have an effect of the binding of anthocyanins to HSA.

Item Type:	Article
Refereed:	Yes
Divisions:	Interdisciplinary centres and themes > Chemical Analysis Facility (CAF) Interdisciplinary centres and themes > Institute for Cardiovascular and Metabolic Research (ICMR) Life Sciences > School of Chemistry, Food and Pharmacy > Department of Food and Nutritional Sciences > Human Nutrition Research Group
ID Code:	32938
Uncontrolled Keywords:	anthocyanin, binding affinity, fluorescence, Human Serum Albumin
Publisher:	Elsevier

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

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