A thermodynamic study of the binding of linear and cyclic oligosaccharides to the maltodextrin-binding protein of Escherichia coli

Biophysical Chemistry
J ThomsonF A Quiocho

Abstract

Isothermal titration calorimetric (ITC) studies over a range of temperatures of the binding of maltose, maltotriose, maltotetraose and beta-cyclodextrin to the maltodextrin-binding protein (MBP) of Escherichia coli are reported. The binding constants of maltose, maltotriose and beta-cyclodextrin are not very different, namely 8.7 x 10(5), 13.0 x 10(5) and 2.55 x 10(5) M-1, respectively at 25 degrees C. The calorimetric data obtained with maltotetraose cannot be interpreted in terms of a definite binding constant. The binding of maltose and maltotriose is endothermic with a large entropy increase while that of beta-cyclodextrin is exothermic, with a smaller entropy increase. The binding of maltotetraose was endothermic or exothermic depending on the temperature.

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Citations

Oct 6, 1999·Current Opinion in Chemical Biology·A Cooper
Apr 26, 2001·Proceedings of the National Academy of Sciences of the United States of America·J S Marvin, H W Hellinga
Jan 30, 2007·Journal of Bacteriology·Samuel A ShelburneDar-Chone Chow
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