Hydrolyzable tannin structures influence relative globular and random coil protein binding strengths
Deaville, E., Green, B., Mueller-Harvey, I., Willoughby, I. and Frazier, R. (2007) Hydrolyzable tannin structures influence relative globular and random coil protein binding strengths. Journal of Agricultural and Food Chemistry, 55 (11). pp. 4554-4561. ISSN 0021-8561
Full text not archived in this repository.
To link to this article DOI: 10.1021/jf063770o
Binding parameters for the interactions of pentagalloyl glucose (PGG) and four hydrolyzable tannins (representing gallotannins and ellagitannins) with gelatin and bovine serum albumin (BSA) have been determined from isothermal titration calorimetry data. Equilibrium binding constants determined for the interaction of PGG and isolated mixtures of tara gallotannins and of sumac gallotannins with gelatin and BSA were of the same order of magnitude for each tannin (in the range of 10(4)-10(5) M-1 for stronger binding sites when using a binding model consisting of two sets of multiple binding sites). In contrast, isolated mixtures of chestnut ellagitannins and of myrabolan ellagitannins exhibited 3-4 orders of magnitude greater equilibrium binding constants for the interaction with gelatin (similar to 2 x 10(6) M-1) than for that with BSA (similar to 8 x 10(2) M-1). Binding stoichiometries revealed that the stronger binding sites on gelatin outnumbered those on BSA by a ratio of at least similar to 2:1 for all of the hydrolyzable tannins studied. Overall, the data revealed that relative binding constants for the interactions with gelatin and BSA are dependent on the structural flexibility of the tannin molecule.