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Binding of an oligomeric ellagitannin series to bovine serum albumin (BSA): analysis by isothermal titration calorimetry (ITC)

Karonen, M., Oraviita, M., Mueller-Harvey, I., Salminen, J.-P. and Green, R. J. (2015) Binding of an oligomeric ellagitannin series to bovine serum albumin (BSA): analysis by isothermal titration calorimetry (ITC). Journal of Agricultural and Food Chemistry, 63 (49). pp. 10647-10654. ISSN 0021-8561

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To link to this item DOI: 10.1021/acs.jafc.5b04843

Abstract/Summary

A unique series of oligomeric ellagitannins was used to study their interactions with bovine serum albumin (BSA) by isothermal titration calorimetry. Oligomeric ellagitannins, ranging from monomer to heptamer and a mixture of octamer–undecamers, were isolated as individual pure compounds. This series allowed studying the effects of oligomer size and other structural features. The monomeric to trimeric ellagitannins deviated most from the overall trends. The interactions of ellagitannin oligomers from tetramers to octa–undecamers with BSA revealed strong similarities. In contrast to the equilibrium binding constant, enthalpy showed an increasing trend from the dimer to larger oligomers. It is likely that first the macrocyclic part of the ellagitannin binds to the defined binding sites on the protein surface and then the “flexible tail” of the ellagitannin coats the protein surface. The results highlight the importance of molecular flexibility to maximize binding between the ellagitannin and protein surfaces.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Agriculture, Policy and Development > Food Production and Quality Division > Animal, Dairy and Food Chain Sciences (ADFCS)
Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > School of Pharmacy > Pharmaceutics Research Group
ID Code:47797
Publisher:American Chemical Society

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