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Size and molecular flexibility affect the binding of ellagitannins to bovine serum albumin

Dobreva, M., Green, R.J., Mueller-Harvey, I., Salminen, J.-P., Howlin, B.J. and Frazier, R. ORCID: (2014) Size and molecular flexibility affect the binding of ellagitannins to bovine serum albumin. Journal of Agricultural and Food Chemistry, 62 (37). pp. 9186-9194. ISSN 0021-8561

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To link to this item DOI: 10.1021/jf502174r


Binding to bovine serum albumin of monomeric (vescalagin and pedunculagin) and dimeric ellagitannins (roburin A, oenothein B, and gemin A) was investigated by isothermal titration calorimetry and fluorescence spectroscopy, which indicated two types of binding sites. Stronger and more specific sites exhibited affinity constants, K1, of 104–106 M–1 and stoichiometries, n1, of 2–13 and dominated at low tannin concentrations. Weaker and less-specific binding sites had K2 constants of 103–105 M–1 and stoichiometries, n2, of 16–30 and dominated at higher tannin concentrations. Binding to stronger sites appeared to be dependent on tannin flexibility and the presence of free galloyl groups. Positive entropies for all but gemin A indicated that hydrophobic interactions dominated during complexation. This was supported by an exponential relationship between the affinity, K1, and the modeled hydrophobic accessible surface area and by a linear relationship between K1 and the Stern–Volmer quenching constant, KSV.

Item Type:Article
Divisions:Life Sciences > School of Agriculture, Policy and Development > Department of Animal Sciences > Animal, Dairy and Food Chain Sciences (ADFCS)- DO NOT USE
Life Sciences > School of Chemistry, Food and Pharmacy > School of Pharmacy > Pharmaceutics Research Group
ID Code:37617
Publisher:American Chemical Society


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