Hydrolyzable tannin structures influence relative globular and random coil protein binding strengths

Deaville, E., Green, B., Mueller-Harvey, I., Willoughby, I. and Frazier, R. ORCID: https://orcid.org/0000-0003-4313-0019 (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 doi: 10.1021/jf063770o

Abstract/Summary

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.

Item Type	Article
URI	https://reading-clone.eprints-hosting.org/id/eprint/8461
Item Type	Article
Refereed	Yes
Divisions	Life Sciences > School of Chemistry, Food and Pharmacy > School of Pharmacy > Pharmaceutics Research Group Life Sciences > School of Agriculture, Policy and Development Life Sciences > School of Chemistry, Food and Pharmacy > Department of Food and Nutritional Sciences > Food Research Group
Uncontrolled Keywords	hydrolyzable tannin, polyphenol, protein, albumin, gelatin, isothermal, titration calorimetry, PROLINE-RICH PROTEINS, BOVINE SERUM-ALBUMIN, NONCOVALENT COMPLEXES, MOLECULAR RECOGNITION, CONDENSED TANNINS, POLYPHENOL, MICROCALORIMETRY, PRECIPITATION, DENATURATION, PROCYANIDIN
Publisher	American Chemical Society
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