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Biomacromolecules. 2011 Mar 14;12(3):710-5. doi: 10.1021/bm101341s. Epub 2011 Jan 20.

Binding of pentagalloyl glucose to two globular proteins occurs via multiple surface sites.

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Chemistry and Biochemistry Laboratory, Animal Science Research Group, Department of Agriculture, University of Reading, P.O. Box 236, 1 Earley Gate, Reading, RG6 6AT, United Kingdom.


The interaction between pentagalloyl glucose (PGG) and two globular proteins, bovine serum albumin (BSA) and ribulose-1,5-bisphosphate carboxylase oxygenase (rubisco), was investigated by isothermal titration calorimetry (ITC). ITC data fit to a binding model consisting of two sets of multiple binding sites, which reveal similarities in the mode of binding of PGG to BSA and rubisco. In both cases, the interaction is characterized by a high number of binding sites, which suggests that binding occurs by a surface adsorption mechanism that leads to coating of the protein surface, which promotes aggregation and precipitation of the PGG-protein complex. This model was confirmed by turbidimetry analysis of the PGG-BSA interaction. Analysis of tryptophan fluorescence quenching during the interaction of PGG with BSA suggests that binding of PGG leads to some conformational changes that are energetically closer to the unfolded state of the BSA structure, because small red shifts in the resulting emission spectra were observed.

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