Interactions of tea tannins and condensed tannins with proteins

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Frazier, R. A. ORCID: https://orcid.org/0000-0003-4313-0019, Deaville, E. R., Green, R. J., Stringano, E., Willoughby, I., Plant, J. and Mueller-Harvey, I. (2010) Interactions of tea tannins and condensed tannins with proteins. Journal of Pharmaceutical and Biomedical Analysis , 51 (2). pp. 490-495. ISSN 0731-7085 doi: 10.1016/j.jpba.2009.05.035

Abstract/Summary

Binding parameters for the interactions of four types of tannins: tea catechins, grape seed proanthocyanidins, mimosa 5-deoxy proanthocyanidins,and sorghum procyanidins (mDP=17), with gelatin and bovine serum albumin (BSA) have been determined from isothermal titration calorimetry data. Equilibrium binding constants determined for the interaction with gelatin were in the range 10(4) to 10(6) M-1 and in the order: sorghum procyanidins > grape seed proanthocyanidins > mimosa 5-deoxy proanthocyanidins > tea catechins. Interaction with BSA was generally weaker, with equilibrium binding constants of <= 10(3) M-1 for grape seed proanthocyanidins, mimosa 5-deoxy proanthocyanidins and tea catechins, and 10(4) M-1 for the sorghum procyanidins. In all cases the interactions with proteins were exothermic and involved multiple binding sites on the protein. The data are discussed in relation to the structures and the known nutritional effects of the condensed tannins.

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Item Type Article
URI https://centaur.reading.ac.uk/id/eprint/5863
Identification Number/DOI 10.1016/j.jpba.2009.05.035
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 > Department of Animal Sciences > Animal, Dairy and Food Chain Sciences (ADFCS)- DO NOT USE
Life Sciences > School of Chemistry, Food and Pharmacy > Department of Food and Nutritional Sciences > Food Research Group
Uncontrolled Keywords Condensed tannin; Polyphenol; Protein; Albumin; Gelatin; Isothermal titration calorimetry
Publisher Elsevier
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