Мақола

Binding of Pentagalloyl Glucose to Two Globular Proteins Occurs via Multiple Surface Sites

Marina A. DobrevaChemistry and Biochemistry Laboratory, Animal Science Research Group, Department of Agriculture, University of Reading, P.O. Box 236, 1 Earley Gate, Reading, RG6 6AT, United KingdomRichard A. FrazierDepartment of Food and Nutritional Sciences, University of Reading, P.O. Box 226, Whiteknights, Reading, RG6 6AP, United KingdomI. Mueller‐HarveyChemistry and Biochemistry Laboratory, Animal Science Research Group, Department of Agriculture, University of Reading, P.O. Box 236, 1 Earley Gate, Reading, RG6 6AT, United KingdomLuke A. CliftonISIS Pulsed Neutron and Muon Source, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Science and Innovation Campus, Didcot, OX11 0QX, United KingdomAn GeaChemistry and Biochemistry Laboratory, Animal Science Research Group, Department of Agriculture, University of Reading, P.O. Box 236, 1 Earley Gate, Reading, RG6 6AT, United KingdomRebecca J. GreenReading School of Pharmacy, University of Reading, P.O. Box 226, Whiteknights, Reading, RG6 6AP, United Kingdom

2011en

ABI

Аннотация

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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DOI: 10.1021/bm101341s

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