Статья

Hydrolyzable Tannin Structures Influence Relative Globular and Random Coil Protein Binding Strengths

E. R. DeavilleChemistry & Biochemistry Laboratory, Department of Agriculture, University of Reading, P.O. Box 236, Earley Gate, Reading RG6 6AT, and School of Pharmacy and Department of Food Biosciences, University of Reading, P.O. Box 226, Whiteknights, Reading RG6 6AP, and Polymer Laboratories Ltd., Essex Road, Church Stretton, Shropshire SY6 6AX, United KingdomRebecca J. GreenChemistry & Biochemistry Laboratory, Department of Agriculture, University of Reading, P.O. Box 236, Earley Gate, Reading RG6 6AT, and School of Pharmacy and Department of Food Biosciences, University of Reading, P.O. Box 226, Whiteknights, Reading RG6 6AP, and Polymer Laboratories Ltd., Essex Road, Church Stretton, Shropshire SY6 6AX, United KingdomI. Mueller‐HarveyChemistry & Biochemistry Laboratory, Department of Agriculture, University of Reading, P.O. Box 236, Earley Gate, Reading RG6 6AT, and School of Pharmacy and Department of Food Biosciences, University of Reading, P.O. Box 226, Whiteknights, Reading RG6 6AP, and Polymer Laboratories Ltd., Essex Road, Church Stretton, Shropshire SY6 6AX, United KingdomIan WilloughbyChemistry & Biochemistry Laboratory, Department of Agriculture, University of Reading, P.O. Box 236, Earley Gate, Reading RG6 6AT, and School of Pharmacy and Department of Food Biosciences, University of Reading, P.O. Box 226, Whiteknights, Reading RG6 6AP, and Polymer Laboratories Ltd., Essex Road, Church Stretton, Shropshire SY6 6AX, United KingdomRichard A. FrazierChemistry & Biochemistry Laboratory, Department of Agriculture, University of Reading, P.O. Box 236, Earley Gate, Reading RG6 6AT, and School of Pharmacy and Department of Food Biosciences, University of Reading, P.O. Box 226, Whiteknights, Reading RG6 6AP, and Polymer Laboratories Ltd., Essex Road, Church Stretton, Shropshire SY6 6AX, United Kingdom

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Аннотация

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 (approximately 2 x 10(6) M(-1)) than for that with BSA (approximately 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 approximately 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.

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Идентификаторы

DOI: 10.1021/jf063770o

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