Binding of an Oligomeric Ellagitannin Series to Bovine Serum Albumin (BSA): Analysis by Isothermal Titration Calorimetry (ITC)

  • Karonen M
  • Oraviita M
  • Mueller-Harvey I
 et al. 
  • 17


    Mendeley users who have this article in their library.
  • 13


    Citations of this article.


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.

Author-supplied keywords

  • interactions
  • molecular size
  • polyphenol
  • protein
  • thermodynamics

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document


  • Maarit Karonen

  • Marianne Oraviita

  • Irene Mueller-Harvey

  • Juha Pekka Salminen

  • Rebecca J. Green

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free